Transcript for:
Biomolecules and Enzymes Lecture from Victory Batch

hello my dear students and welcome back to victory badge and i am your dikshaman so today we are going to start with the most awaited chapter that is biomolecules a very very very important chapter because it is also in the class 12 but in the chemistry section anyways let's get started with this first of all before starting this chapter what is a biomolecule so you must have heard of this many times because that's in your syllabus first of all what is a biomolecule so biomolecule are all the elements of the molecules that are present in a living system or in a living cell whether it's organic or it's inorganic but mostly we consider the organic molecules as biomolecules so these are the molecules present in the living organism present in the living organisms okay so these biomolecules they are usually we call them as the organic ones and um you know without them your body cannot be you know the way it is in fact you are completely made up of biomolecules they are completely made of biomolecules but how do we get to know that what biomolecules do we contain so let's get started with a very simple experiment and that is how to analyze the chemical composition so how can we see whether a tissue have what chemicals in it so with that we have done a very simple experiment what is that we took some tissue and this tissue is for example a liver tissue okay you can also take a plant tissue since i am a zoology teacher so we'll be taking a liver tissue so we took the liver tissue here right and then we grind it and then we grind it in mortar and and we also added trichloro acetic acid we also added trichloroacetic acid and we grind it and grind you know what is a mortar and pestle you know in your homes there are a certain small even made up of marble or stone or uh marble is already stone or iron things motor and pestle where you grind these spices and sometimes ginger for the tea right so that mortar and pestle it contains the tissue and tissue is grinded in it and we are also adding an acid in it which is trichloroacetic acid so by this a slurry is formed that means um you know mixture kind of a stuff is formed and now you are going to filter it now what you are going to it filter it so when you filter this one for example this is a funnel and with the help of funnel you filter it okay we added a cheese cloth or a cotton or cotton in this for filtering just like you do in your laps whenever you have to filter you add a filter paper but at that time they didn't add the filter paper they added cheese cloth or cotton and they started filtering the slurry okay what did they added they added slurry and what they find out that what they find out that some component of slurry remains here and some component comes down here in the beaker the molecules or these the part of the slurry that remains in the or that retains in the funnel you call it as re-tentate what you call it as re-tentate and the one that get filters out here is the filtrate this one is a filtrate okay now why you call it and call it as retented and filtrate or why some left some of the molecule they're left on the filtration membrane or here in the filter filter paper or whatsoever cheese cloth is and why others caught filtrate there is a reason because the molecules which can easily get mixed in the acid it can get filtered easily and the molecule which cannot get mixed with the acid which i said this trichloro acetic acid they remains up unfiltered okay now why a molecule or why another molecule is not getting you know dissolve in an acid first reason it's chemical property second reason it's size for example if i say mix salt mix salt and sugar in the water okay which one will uh get dissolved obviously salt because the molecules are small and according to the chemical property they will get mixed easily but sugar will take some time or what if i take some other things which are very large molecules they will also not get mixed so all those things which can you know mixed easily in the acids they come under acid soluble pool so acid soluble pool contains a very small size molecules known as bio micro molecules micro means small molecules they can easily dissolve in the acid so they're acid soluble and that's why they got filtered here along with the acid but the one which are larger in size they cannot get dissolved in the acid so they come into the acid insoluble pool and since they are larger in size that's why they were not able to get dissolved okay and they come under the retented form now what a bio macro and micro molecule first of all we have divided them on the basis of size so we say that bio micro molecules are the molecules which have molecular weight of which have molecular weight of less than 1000 dalton dalton is a unit just like we say kg and grams and what are bio macromolecules they have molecular weight of more than 10 000 dalton so all the polymers they come under the category of macromolecules and all the uh you know monomers they come under the category of micro molecules so you must have heard that starch and glycogen are polymers so they are formed from glucose which is a monomer okay so your simple sugars what guys your simple sugars they come under the category of bio macro molecule in fact your amino acid they also come under the category of bio micro molecule and your your nucleotides they also come under the category of bio micro molecules let's polymerize them simple sugars they polymerize okay they polymerize to become complex sugars right amino acid they polymerize to become proteins and nucleotides they polymerize to form nucleic acid like your dna and rna they come under the category of macromolecule also lipid according to this experiment comes under the category of bio macromolecule but lipid have a controversy lipid have a controversy now what's that controversy is we say that lipid is not a strict bio macromolecule we say lipid is not a strict bio macromolecule what does it means though according to this experiment though according to this experiment we have kept it in the category of the macromolecule but why it's not a strict macromolecules the reason is if we see according to molecular weight if we see according to molecular weight its molecular weight is less than 800 dalton so technically okay let me write it nicely 800 dalton so technically it should be a bio micro molecule but if you'll see the chemical property it comes in the retentate so that's why re 10 8 right so technically this is the one this is the one which is a strict which is not a strict biomacro molecule so it's between the two so nowadays if we classify them according to molecular weight definitely lipids will come under the category of micro molecules okay all right now why it is coming under the retentate the reason is white is coming under the retentate the reason is when if for example this is a cell okay this is a cell and this is a cell membrane and cell membrane is the one which contains maximum lipids all right and you all know lipids they're present in this form here in the form of this right so when you will destroy the cell membrane all these lipids fatty acids or the of or the entire lipid structure what it will do it will make the small vesicles like structure round vesicles like structure and this surround vesicle like structure it is not soluble in the acid acid right so you heard it right so these vesicles are formed right or these lipid vesicles are formed which are insoluble in acid so hence we say that it comes under the category of redempted all right so that's the reason why during the experiment lipids were there in the indented all right okay so let's get started with the another experiment so this was about what is present okay so we are talking about basically the organic molecules now what are organic molecules the one which have carbon in them the one which have carbon in them they are organic molecules but what about the others what about the others there are a lot of things also present do we don't we have calcium don't we have sodium we have a lot of other you know inorganic elements in us also so to check the inorganic elements we perform this experiment known as ash analysis so what we do in ash analysis so nash analysis first of all we take the tissue like we have we took the plant tissue okay now we weigh it and you call it as wet way we took its weight because it has water in it so that's a bit weight right now after that we dry it after drying the all or the excessive water is uh you know it goes away so now you again take away and that is dry weight right now what will you do you will burn these tissue completely you burn it completely so when you will burn it what will happen so when you will burn it the carbon containing organic molecules carbon containing organic molecules they will be vanish how they will form co2 and water and that will evaporate okay now whatever is left whatever is left is ash and this ash it contains inorganic elements inorganic elements so if you know when someone dies especially in hinduism the that person is burnt completely right in the funeral or right and you call it as basically the incrementation okay so what happened what is left after the person is completely burnt or the body of a person is completely burned the only thing left is that ash which contains some part of the bones right the bones organic matter goes away and inorganic that is one with the calcium it will it it gets left and the other things that to get vanish away fine so here all these inorga inorganic elements can be studied by studying this ash okay now what are the various inorganic elements present so it can be sodium potassium calcium magnesium water and other compounds so now what is the use of these elements in our body so you all know sodium and potassium this helps in the nerve impulse it helps in nerve impulse and it also make or it also maintain the electrolyte balance right calcium calcium have a number of roles that have a number of roles let me tell you some of them first of all calcium helps in blood clotting calcium is a part of bone calcium also helps in muscle contraction it also helps in muscle contraction what about magnesium magnesium is acting as a cofactor with enzyme will study cofactor in this chapter only you know how does enzyme work enzyme convert one thing into the another they catalyze the reaction but sometimes enzymes are incomplete enzymes are incomplete without certain things they are co factors they will not work without them so magnesium along with enzyme it helps in catalyzing the reaction okay water is the basis of chemical reactions bases or medium of all the reactions without that no reaction can take place and then we have nscl for electrolyte balance calcium carbonate calcium phosphate for bones again phosphate and then we have these dibasic ions that will helps in maintaining the ph of solution so for maintaining the ph we have die basic we have dibasic or and monobasic ions right they help in ph balance and whatever balances the ph you call them as buffer so they are acting as buffers so see inorganic elements also play a major role right okay now you have seen this chart in ncrt no all right okay so there is a comparison between the earth crust and human body what elements do we have and what elements earthquakes have so you need to memorize them okay if you can it's really nice uh the what are the most important thing to memorize i'll let you know now so first of all hydrogen so in earth crust hydrogen is 0.14 so it's very tough to remember everything okay so what first of all you have to do which is the most abundant in us that is oxygen and which is most abundant in the earth crust that is again oxygen so both in oxygen or sorry both in earth crust and our human body oxygen is the most abundant and again if we compare both we have more oxygen 65 percent and this is 46.6 percent so this is earth crust that means the land it's not about the atmosphere okay second thing which is the second most abundant okay let's find this out in human body that's carbon in human body that's carbon now let's uh see what's the second most abundant in the earth crust that's silicon the thing which is second most abundant in the earth is negligible in us is negligible in us okay so by this way you can learn this entire chart and the things which i have circled these are most important all right so moving further let's talk about primary and secondary metabolite so to understand primary and secondary metabolite you need to understand one term that is metabolism what is metabolism total of all the chemical reactions sum total of all the chemical reactions in our body so for example right now your body is performing a role of glycolysis it's also digesting your food and whatever reactions are taking place just total them up and that will be your metabolism and whatever elements organic molecules are participating in it they are metabolites for example i say glucose gets converted into glucose 6-phosphate so glucose is also metabolite glucose 6-phosphate is also a metabolite or i say glucose get converted into pyruvic acid so glucose and pyruvic acid they both are metabolites so whatsoever things are used in metabolism they are metabolites metabolites are what molecules used in metabolism and they are again usually organic molecules so when we are talking about metabolites they are majorly organic molecules okay now there are two types of metabolites guys there are two types of metabolites one are primary another is secondary now what's the literal meaning of primary and secondary whenever i'm saying this is my primary work i mean that this is most important to me if i say this is secondary that means it's not much important to me okay for example if i say in my whole day in my whole schedule my primary work is to do the teaching right is to do my uh this job work so that means that that is more important to me my secondary can be some other things like my household work it can be like anything like a watching movie or something like that okay so primary work is something or the primary metabolites basically primary metabolites are something if they get away from your life you will or from the organism the organism will not be able to survive okay so primary metabolites are those metabolites if you will take away from the animal animal will not survive like if i say i take chlorophyll from a plant plant will not survive how does it will do photosynthesis and produce food or if i take glucose from the plants or if i take certain enzyme from the plants that are helping in photosynthesis they all are primary metabolites not the enzymes sorry the substrate so all these things are very important for the plant all the metabolites in photosynthesis respiration they are very important for the plant so if you take away from them they will eventually die but there are certain metabolites if you take away from the plant might be they will not die for example if i say if i take carotenoids which is also a pigment take if i take that away from the plant maybe the plant will not die because in its leaf chlorophyll is present that will produce food but these pigment have some other roles which are secondary roles okay so the plant like carrot plant okay have two pigments in the carrot we have carotenoid and in its sleeve we have chlorophyll now what out of these two is a primary and secondary chlorophyll is primary because that will produce food and carotenoid is not producing food so it can be secondary okay so primary metabolites are those metabolites that are very important that are very important for normal physiology what is physiology body functions normal physiology or function okay and this one not much important for normal physiology all right so if i take away primary metabolite the plant can die the plant can die without them the secondary metabolites though they can have certain roles i don't say they don't have any roles like we say carotenoids might protect it from the sunrise okay but if you take them away might be the plant will not die a little of it can be affected so might be they will be having certain functions maybe that are not good for the plant or that are not that good for the plant that the plant cannot be able to survive okay all right so now what are the secondary metabolite second thing that i want to add here is that whenever i'm talking about primary and secondary metabolite that means we are talking about plants bacterias we are not talking about animals animals do not produce any secondary metabolite okay so let's see what are the various secondary metabolite and from neet point of view this is quite important let's get started okay so first of all we have pigments so in pigments we have carotenoids and enthusiasm alkaloids morphine and codeine for plants morphine and codeines are alkaline they may be you know is useless you know some alkaloids in the plant have one purpose that that makes that plants taste less the animal will not be able to eat but is that so much essential for the normal physiology of plant no it's like chance if the animal will eat it will eat otherwise it's not doing much for the plant okay but for human being they have a function morphine is a powerful painkiller and codeine is used in cough syrups it's used in cuff syrups terpenoids monoterpenes and dieter peens these are certain kind of components which produce you know certain kinds of oils and aromatic compounds in the plants then we have essential oils lemongrass oil these oils nowadays are very much in demand because they are so much important in the hair growth in the skin yes they are very important for skin like tea tree oil that's uh that is very good for acne whosoever have acne that that they can apply toxins like abraham and ricin these are toxins which if it is eaten by the animal animal will die again a defense mechanism for the plants lectins are not for plants that is for bacteria it's present in the wall of bacteria and it is useless for the bacteria but if the bacteria enters into our body corn canvalene a is identified by our immune system and immune system will kill the bacteria so rather than being useful it is useless right or it can be like a killer thing for bacteria drugs when blasting which is anti-cancerous curcumin is present in curcuma longa which is your healthy turmeric right and then your polymeric substances like rubber gums and cellulose now you must be thinking i'm cellulose yes so cellulose acid is not doing a lot of function in the plants maybe it's increasing the strength of the cell but not that important for the cell okay so all these are secondary metabolites guys let's move further and talk about the carbohydrates carbohydrates so what does it have carbon as its name have carbon and hydrates that is water so we say that they are hydrates of carbon hydrates of carbon why what's the ratio of hydrogen and oxygen in water what's the ratio of hydrogen and oxygen in water 2 is to 1 so same ratio is in the in the carbohydrate okay you can find the same ratio of hydrogen and water in the carbohydrates that's why you call it as hydrates of carbon they are also known as sugars or saccharides they are also known as sugar or saccharides okay so if i talk about the carbohydrates so how do they look like so first to see how the carbohydrates they look like we need to see the structure of glucose okay so they are made up of carbon and if i talk about glucose it is c6h12o6 okay and here if it is c6 you have to draw six carbon one two three four five and six this is how you make the structure of glucose you have to follow me side by side draw six carbon one two three four five and six ron in the row now on the last carbon draw h2oh and on the first one draw here c h o like this okay so now here the first carbon have the group cho that is an aldehyde group so we say that our these carbohydrates they are polyhydroxy eldosis poly hydroxy eldoses or ketosis what does it means that means either the sugar will be having the main group that is the aldehyde or it can also contain the group ketone right so for example the structure we have drawn so far the part half structure we have drawn so far is of a glucose so glucose have aldehyde group so the example of a polyhydroxyl dose sugar is glucose similarly we have another six carbon sugar that is your ketonic sugar fructose right so fructose will be having the ketone as a you know a main group here or a functional group and the glucose will be having the aldehyde as of main group if you'll see how many carbons do have both have six carbon both are c6 h2lo6 right but these are isomers they have different types of you know structure due to ketone group now now let's see here let's complete the structure now on the third carbon h will be on right side and everywhere else o h will be on right side like this and wherever you have o h put h in front of that you know carbon have uh carbon have uh you know four valences so we want to satisfy its four valency so now you can see on the fifth carbon oh is on the right side so this is a dextro rotatory glucose d glucose if it would be a mirror image and o h was on the left side then this should be l glucose l means levodora tree so d means dextro rotatory extro rotatory the detail of this you will be doing in the chemistry one in class 12 okay now let's draw the cyclical structure this structure is a linear structure with the this uh main group that is aldehyde one more thing that i want to add here we say that it's polyhydroxy what is hydroxy means o h group so it has a number of o oh groups that's why it is polyhydroxy second thing guys here the carbon which have the main group which have the main group attached to it which is the aldehyde group or the carbon which is participating in the formation of main functional group that carbon is known as carbonyl carbon what you call that carbon as carbonyl carbon okay now let's draw the cyclical structure so if we'll see here how does a cyclical structure is formed all right so what happened the carbon one and carbon five they have an affair all right so now they are going to join to each other and they're going to form this ring they're going to do a the you know reaction here and they're going to form a ring-like structure now you can see in this ring six carbon is not participating so it is out of the ring it is out of the ring so the ring formed is hexagonal and this type of a rings are known as pyro nose rings so pyrenose rings are the rings that are six sided rings okay so this o oxygen is uh from one of them why because they are going to react now you can see here this is first carbon this is second this is third this is fourth this is fifth and where will be the sixth one because it is not participating it will be outside the ring so this is how it is fine so the first carbon is a carbonyl carbon so when they are reacting so whenever they are reacting so this is how first carbon will come out here right so h here is in the downside here h will be on the upper side like that here o h is on the downside here o h is on the upper side h on the lower side again h on the upper side o h on the lower side how will i get to know that you can see oh they're alternative okay they're altering uh in an alternative fashion now what about the first carbon in first carbon you cannot predict right now there are two types of rings formed there are two types of rings form so one is alpha ring another is beta ring one is alpha ring another is b turning both the rings are similar in this structure second third fourth fifth and sixth carbon will exactly be similar the only difference between alpha and beta ring will be on the basis of first carbon on the basis of first carbon if first carbons o h is below the ring and h is on the above the ring this will be alpha glucose so in alpha glucose o h is always below the ring right let's see how beta looks like so for that let's see the structure of ribose so ribose have five carbon one two three four and five so here also the bond is formed between first and fourth carbon and the ring is five-sided because it has less carbons and the five-sided ring is known as furanose ring is five-sided so here you can see first carbon and fourth carbon are sorry first carbon and fourth carbon are making bonds so this is how they are and fifth one you can see it is outside the ring so this is the fifth carbon this is second this is third so as you can see as comparison to the earlier one i have told you always the difference between the uh the alpha and beta ring will be on the basis of first carbon only because that's the carbonyl carbon main carbon so here also the first carbon have oh on the above side so that's why this ring is beta ring so here you can see on the first carbon h is on the below the ring so it is the alpha glucose okay so alpha and beta rings can be formed in any type of a sugar in the ring structure form the only difference is on the carbonyl carbon which or where the which is present if it is above the ring its beta if it is below the link it is alpha right okay moving further to the derived monosaccharide so what are derived monosaccharide these are monosaccharides that have been derived from the another monosaccharide okay what what is monosaccharide saccharide means sugar mono means one only one sugar so for example this is a structure of ribose okay so if i take away oxygen from the second carbon it will be having less one sugar that will become deoxyribose so you must have heard there are two types of sugar one is ribose another is deoxyribose and you you must have heard the deoxyribose is present in the dna and ribose is present in the rna okay so when you remove o or oxygen from the second carbon of the dibose this sugar become deoxyribose so because we have derived this sugar from the ribose so that's why you call it as deoxyribose sugar and deoxyribose is present in dna and this is present in rna and in fact in adp adenosine triphosphate all right okay that's about the derived sugar let's talk about disaccharide now what is a monosaccharide one single sugar is a monosaccharide what is a disaccharide when two sugars s one s two for example this is one glucose there is another glucose they react and they join each other via some bond and by uh or leaving or by you know by removing one water molecule this type of a sugar is a disaccharide so two sugars are involved they're joining each other and they are joining each other with the help of a glycosidic pond which want glycosidic bond so this type of a sugar will be known as the disaccharide because it has two sugar now if you compare if i talk about s1 and s2 together and this one and this one s1 and s2 which will be having more carbons sorry which will be having more uh hydrogens yes let me know if i say i have s1 and s2 imagine if i am drawing this uh this sugar is a maltose sugar okay this sugar is a maltose sugar and i say malto sugar is formed by the combination of two alpha glucose it is formed by the combination of two alpha glucose okay so two alpha glucose they are combining and they are forming like g1 and g2 and they are removing water and they're forming this sugar which is the maltose okay now as comparison to this structure to glucose and this structure maltose structure which will be having more hydrogen obviously this will be having more hydrogen why this is c6h12o6 this is c6h12o6 now when you will remove water this structure which is maltose it will be having less oxygen so if you will join them this will be this will become c12 h24 and uh oh 12 right but you have to remove water only then it will become maltose now what will be the structure of total number of carbons in the maltose-12 you have to remove two hydrogen that will be h20 and you have to remove one oxygen that will be o11 so this is the chemical structure of your uh maltose fine and this is how it looks like so you can see this is one glucose this is another glucose and they have been bonded so if you'll see here guys clearly uh this one is your first carbon this is second carbon this is third carbon this is fourth carbon fifth carbon and six carbon okay now this one is also glucose so similarly first carbon second carbon third carbon fourth carbon fifth carbon and six carbon okay so when you want to remove water so which carbons are involved in removing water the first and the fourth that's why the bond has been formed that's where the bond has been formed so this bond is technically c o c bond you call it as glycosidic bond this is glycosidic bond so we always name these bonds on the basis of what carbon have been involved what carbon have been involved okay so if you do not understand this let me tell you earlier here o h was present okay how it was present oh here and over here now let's remove water so this was how water was removed after removal of water only oxygen is left and this is how they have been bonded okay so this is how a glycosidic bond is formed between two uh glucose now because first uh both the glucose they are alpha so i will write alpha okay this is how you name the bond this these both glucose are alpha so i'll write the alpha here the first carbon is involved which is forming bond with the fourth carbon of the another one and this is how i will write the name of the bond alpha 1 4 glycosidic bond alpha 1 4 glycosidic fine okay so this is for sugar maltose maltose is also known as malt sugar and you find this in the germinating seeds germinating seeds in fact you will get surprised to know that whatever drinks you are having like one vita or a complain or malt over horlicks they all have a base of malt sugar or maltose go check your health drinks okay so that's basically sugar all right so that's the first disaccharide that's maltose so second we have is another disaccharide that is lactose so you must have heard of lactose lactose is a milk sugar lacta word is always used for milk so so it's a milk sugar okay so here you can see uh the you can see two sugars are used okay now you must be thinking man they both look like glucose no one of them is galactose let's see so you have seen this earlier diagram oh is below the ring on fourth carbon so this is what your glucose is and in this one if you can see oh is on above the ring on fourth carbon this is first second third and fourth so this is your beta galactose okay and this one is your beta glucose how you came to know that's beta because o h is above the ring okay because this is first carbon second third fourth fifth sixth again this is one two three four five and six now tell me what will be the name of the bond the the entire process is same oh and which will uh will take away or it will remove the water right so here the because sugar is beta so beta one four glycosidic bond all right okay so my lactose is a milk sugar it is formed by the combination of beta galactose plus beta glucose now this is also important with sugar comes first the galactose comes first all right next sugar okay you have to okay so next sugar is your sucrose sucrose is your cane sugar or also known as table sugar because this is the common uh sugar that can be found on your dining tables right so it is obtained from sugar cane that's why its name is cane sugar the one you use in at home okay so this is formed by the combination of two different types of sugars you can see this ring is pyranose it has six sides this is furanose it has five site so this one is your alpha glucose and this one is your beta fructose okay now you must be wondering ma'am but we have done ribose which is uh five-sided how many carbon does ribose have five how many fructose have six let's see first carbon second carbon okay we will start from from here uh this is first carbon this is second carbon this is third carbon this is fourth carbon this is fifth carbon this is six so clearly it's not a ribose okay so this one is fructose now why being having six carbons uh it's not producing same or it is not forming same ring like that of glucose the reason is it is a ketonic sugar it is a ketonic sugar right and this one is a ld height sugar so due to that the ring formation can also get disturbed all right okay so here you can see the uh this is first carbon of your glucose this is second third fourth fifth and sixth so the bond here is formed between first and second carbon so here you can write alpha 1 and beta 2 glycosidic bond because this sugar is beta sugar all right so sucrose is formed by the combination of alpha glucose plus beta fructose all right guys now let's move to the reducing or non-reducing sugar now what is a reducing and on reducing sugar so there is an there is a test in chemistry that is felling benedict test so by performing this test you can identify the sugars how can you identify the sugars we have identified the sugar based on this test into two categories so we have divided the sugars based upon this test into two categories okay so the first is a reducing another is a non-reducing sugar first you need to understand what's the difference between the two so reducing sugar will be the sugar that is basically reducing something that is basically reducing something for example for example if i say this one is blue in color this is how the solution is so when i added the solution when i added one sugar if this sugar can convert can convert the cubric irons the cubric irons of this solution into cubris iron then this uh this solution will become red if the cubric to cupress conversion takes place for example this is the solution when nothing was added and when you added sugar this is how it turns into red so if the solution turns into red we got to know that the cupric ions have been converted into cupress that means it has reduced it it has reduced it so that sugar will be reducing sugar so all the reducing sugars okay all the reducing sugars can convert can convert cupra kinds into cupras okay and this is how they can convert blue to red color of a solution right so any sugar for example i have added x sugar i don't know what that sugar is if i added it in the uh felling benedict uh solution then the solution turns into red from that i'm pretty sure that sugar is a reducing sugar okay now what are the reducing sugar so to uh so to do this conversion we need to have one functional group of a sugar okay we need to have its functional group as free for example monosaccharides have free functional groups what are functional groups guys what are functional groups the functional group is this carbonyl carbon if you have seen in the um if you have seen in the formation of disaccharide always one carbon in carbon is always there for reaction because other groups they can't react other groups they can't react if i ask these two react it will be difficult for them so for reaction we definitely need one carbonyl carbon for the reaction let's just check it out in maltose first carbon is the carbonyl carbon here okay this is carbonyl carbon i'm writing cc so this is uh in the process of the uh reaction okay in this one you can also see the carbonyl carbon is involved that's why the reaction is happening again in this one both carbonyl carbons are involved the fructose carbonyl carbon is second because it is a ketone and in ketone we want groups on either of the side okay so fructose carbonyl carbon is second all right so we say for reaction we need carbonyl carbon all right now this is also a reaction so definitely reducing sugars will be having at least one carbonyl carbon so all monosaccharide have free carbonyl carbon so they are they have a very free carbonyl carbon they can reduce the cubic into cupra sign talking about talking about the disaccharide here the carbonyl carbon of first sugar has been already involved and formed the bond it cannot reduce the cupric ions into q plus one fine so this one is out but this end which is the right end this is also carbonyl carbon so this will lead to the uh conversion of kubrick into cupress so in all if i say the maltose can be a reducing sugar because it has one free carbonyl carbon and this can convert that cubic into cupress similarly in the lactose also this carbonyl carbon is free and it can also cause the change okay now let's talk about this one do they have any free carbonyl carbon no because glucose first carbonyl is already involved fructose have second as a carbonyl carbon this is also involved so the this sugar sucrose it cannot convert cubric ions into cupress so we can put this into the category of non-reducing sugar non-reducing sugar so non-reducing sugar is your sucrose so this is the most common question that is asked okay whereas here monosaccharides and lactose and maltose they are the reducing sugar so why do we do this test for example if you don't know what that sugar is you can identify uh it with that test for example if i say i added and no color change occurs so straight away that's sucrose okay all right now let's talk about polysaccharides poly means many saccharide means sugars so it will be formed by the combination of many sugar units always this left side will be non-reducing just like in maltose the first carbon of the first glucose was involved in bond formation so it will always be non-reducing and the right end is always free with carbonyl carbon so this right and always will be the reducing end okay left end in a in fact in a disaccharide like lactose and maltose and in polysaccharide left hand is non-reducing and right end is always the reducing end why because it has free carbonyl carbon now these homophobia these are sorry polysaccharides they are divided into two categories they are divided into two categories one is homo polysaccharide another is heteropolysaccharide for example in the polysaccharide if all the sugar units are same like if i say these all ss are glucose it's a homo polysaccharide if i say these all are not same but different like one is glucose another is galactose it will be a hetero polysaccharide right so homo polysaccharide they are made up of same sugar units and they are made up of different sugar units let me give an example here peptidoglycan that you do in the in the bacteria the cell wall of bacteria is made up of peptidoglycan that contains two type of sugars nag plus nam now talking about this one homopolysaccharide we have a lot of example like starch like glycogen etc okay now let's get started with the polysaccharide in more detail first we are going to talk about the storage polysaccharide we have divided the polysaccharide on the basis of their function into two categories one is storage storage means they are performing the function of storing something for example starch is a storage polysaccharide so it's a food of plant which is stored in the body glycogen is a storage polysaccharide of animals and bacteria and in fact sometimes fungus so this is a sugar that is stored in our body if i say cellulose it is forming cell wall so it's a part of a structure so that's a structural polysaccharide okay so for storage we have starch starch is formed during photosynthesis formed during photosynthesis all right so if i talk about starch and if i zoom it and i see the structure of starch i will not find a similar type of structure rather in the starch i can find two types of structure one type of a structure is helical and its name is amylose and another type of a structure which is not helical is amylopectin so two types of structures two types of structures are present in the starch one which is helical and unbranched another which is helical but branched right so a milo is helical and branch and unbranched okay so whenever two sugar units are joined in the starch what sugar units are used in the starch alpha glucose right so starch is made up of alpha glucose so that's why you can digest it because for its digestion you have alpha salivary amylase so these alpha glucose when they are present in the straight chain that means there is no branching they are present in a manner of the straight chain like this right so this is how all the molecules are present in the amylose but sometime these chain becomes helical but there is no branching so here the bond will be here the bond will be alpha 1 4 glycosidic bond alpha 1 4 glycosidic bond okay now if i talk about amylopectin here this is how the structure is this is going like straight chain and somewhere here it will start forming bond with the other sugars and it will show a branching like this okay so here it is forming bonds with the adjacent molecules of glucose in a straight chain the bonding will be same which will be alpha 1 4 glycosidic okay so whenever it has to undergo whenever it has to undergo branching here it is going to form the bond like this and this bond is alpha 1 6 glycosidic part okay let me explain you in more detail by using the adjacent picture here this is glucose one this is glucose one glucose two and glucose three both are joined to each other by one four or alpha one four bonding this is the fifth carbon this is the sixth carbon this is the first carbon now as you can see it is showing branching here so here this coc bond is formed here this bond is formed glycosidic bond here this is a glycosidic bond so this bond is basically alpha 1 6 glycosidic so this is how at branching it shows alpha 1 6 bonding okay so now you must have heard that starch gives blue black color with iodine why the reason is the iodine molecules get trapped in the helleses of a milos okay that's why starch gives blue black color color with iodine why because it gets trapped in the helical strands of amylose moving further to the next polysaccharide that is glycogen so it's a storage polysaccharide in animals fungi and even bacteria so this structure is also made up of alpha glucose and this is also a branch structure it is also a branch structure as you can see this diagram of ncrt so this is a straight chain in the straight chain you can see alpha you can see here alpha one four bonding alpha one four bonding alpha one four bonding but if it has to form the bond here it will be alpha one six bonding just like that of starch okay just similar to starch all right guys the only difference is the pattern is different bonding is same the pattern of amylopectin and glycogen is little different but the bonding is same anyways let's move further and talk about the inulin now there is one insulin which is the hormone and now there is inulin that is the storage polysaccharide this is formed by the fructose it is a polymer of fructose it is present in the plants like a tree chalk in tubers of a tree choke you can see a tree choke in the diagram so here you can find this sugar which is inulin so most of you in the exam you get confused with the insulin and inulin or you are in a hurry reading the question at that time may you maybe there can be a possibility you can miss the word s but you don't need to do that okay all right so moving further to the next sugar that is a structural one that's the uh cellulose so cellulose is present in the cell wall of plants it's also the homo polymer homo polymer of beta glucose so now the story changes this is beta glucose that's why you cannot digest cellulose why because you don't have beta amylase you have salivary alpha amylase which can break alpha bonds because this is beta sugar so the bond will be beta bond so here you can see guys what will be the bond first carbon fourth carbon beta one four linkages and it is unbranched structure you can't see any branching here as well it is homopolymer and unbranched okay the cellulose can be used for many purposes cellulose is a like one of the most abundant organic compound in the biosphere okay so if you will see this cellulose is used for various purposes first of all the cellulose can be used for making paper cellulose can be used for making paper cellulose can be used to make rion rion is artificial silk and what do you do with silk you make clothes right natural silk is a protein also you can make cmc carboxymethyl cellulose right to make anything uh from cellulose first you have to convert it chemically by reacting with substances like here you have converted into carboxymethyl cellulose this one is used in cosmetics to give a smooth texture it is also used in drugs as a solvent and it is also used in the ice creams to give a smooth texture okay another thing to note it is also used to make explosives so these are some of the various uses of cellulars okay so next structural is the one you have already done in the cockroach that is skyteam so cartoon is a structure polysaccharide it is made up of n acetyl glucosamine and acetyl glucosamine nag it is a polymer of nag and where do you find it in exoskeleton of arthropods exoskeleton of arthropod and cell wall of cell wall of water okay next it's also homo polymer because it is only made up of one type of a sugar now you must be wondering ma'am what is necessary glucosamine it's a derived sugar like your deoxyribose was also a derived sugar this is also derived sugar with glucose you add amine group and acetyl group that will become n-acetyl glucosamine all right my dear students it's time for you to do some practice of questions which of the following is not present in acid insoluble fraction not present in the acid insoluble fraction it will be of the acid soluble one protein are complex they are the part of acid insoluble nucleic acid are the part of the insoluble lipids are also the part of biomacro molecule whereas glucose is a monomer so it's the part of acid soluble fraction next cellulose is a heteropolymer made up of glucose and galactose no homo polymer very true but not of alpha glucose homo polymer made up of bleta glucose hydropolymer it is not so answer is third next inulin is a polymer of very straightforward question you can never get such kind of question if you get that an exam maybe it can be in the form of match the following so you must be lucky then match the following as i have told you first alkaloid which is alkaloid in this one codeine lectin is con canvalin a drug is curcumin toxin is abrin and ricin all right next we are going to start with this amino acid guys what are amino acid so amino acids are technically your substituted methane what are these substituted methane substituted methane what is a methane methane is ch4 let's draw so carbon with four hydrogen but we have substituted it with some other uh you know groups like hydrogen it can be nh2 and here coh and here this is the r group which varies with the amino acid because they are of different types fine so this carbon is the alpha carbon because it contains all the group together and this is how you called all amino acid as alpha amino acids alpha amino acid amino because have it has amine group acid because it has one acetic group now there are total total 20 protein forming amino acid now there is a difference number of amino acids are many but the one which forms protein they are only 20. so we have in all around 20 protein forming amino acid amino acid that participates in the formation of proteins fine now so here our group can differ in the different types of amino acid that we'll be talking about that shortly now let's talk about the chemical property of amino acid so amino acids chemical property depends upon only one thing that is not obviously a number of thing one one thing or one property that actually causes a lot of change in the function of amino acid is the ph of solution what ph so ph of solution uh can cause uh the hyperactivity or hypoactivity of the amino acid how let's see amino acid can act as uh you know as a cationic form or an anec form according to to the ph of solution according to the ph of solution so for example if i say this is the basic structure of amino acid okay so imagine this is in the low ph state the ph of solution is low so now it will take up one hydrogen ion from the solution because low ph have more h positive ion and it will act as a cationic form so i will say at low ph the amino acid work as a cationic form now if i if i increase the ph it like moves above seven so at that ph it can act as an ionic form it will act as anionic form so it will act as the anionic form when the ph is high now when i am changing the ph when i'm changing the ph from low to high in between that a ph will come where the amino acid is working or it is acting as both anionic and cationic form it is acting as both an ionic or cationic form that is i can say dibasic iron all right so i can say that here it is acting as both a 9 as well as catin both anion and cationic form okay so dynamic form so i will call this now as a zwittering what do you call it as zwitterine zwitter means hybrid so it is a hybrid between the two here i can see that it is both an ionic and cationic form all right guys okay so it is acting as both uh the kitanin and ionic form the ph at which it for it act as a zwitterine you call it as isoelectric ph you call it as isoelectric ph or isoelectric point now let's talk about the various classification of amino acid so now that's a lot thing but very important thing okay so first classification that we do is according to the structure now if in the structure if in the structure the r group as i say the r group is different in all the amino acid if the r group is something like hydrogen or ch3 or ch2ch3 then this kind of amino acids will be in the category of neutral the neutral volume do not have any extra group they have one nh to one sewer in the entire structure and these type of r groups can be present like in glycine h is present okay let me show you here okay so as you can see this is glycine alanine valine isoleucine and nucin all comes into the category of neutral amino acid right so as you can see here they have only one coh one nh3 this is in the cationic and the ionic form zetaline state so they have written in this manner just focus on the r group r group is h in glycine ch3 in ln and ch ch3ch3 in the berlin so these type of groups are present in all the uh amino acids so they comes into the neutral now let me talk about acidic so as you can see in acidic amino acid this one the we have aspartate and glutamate so you can see there are two co negative groups so both are the like having more acidic charge here so or more acidic groups are present so they will be treated under the category of acetic amino acid now let's talk about the basic one the basic one we have is lysine and arginine you can see here there are two nh3 groups ns3 gives you a basic in fact here we have three so anyone which have an extra nh3 group they are treated in the category of basic amino acid now if i say someone have oh group like this then they will serene and throne in they will be treated under the category of alcoholic amino acid and now if anyone have sulfur like cysteine have sulfur methionine have sulfur they are under the category of sulfur amino acid all right now if any have any of them have a rings like aromatic rings they are aromatic amino acid right so anyone that have the heterocyclic ring what a heterocyclic ring the one which does the ring which is not just made up of carbon aromatic ring this one is made up of carbon all are carbon heterocyclic have nitrogen in it so that will be in the heterocyclic one right so let's go back so in neutral amino acid we have gavel learn it from gavel gavel is uh this is one letter abbreviation this is one letter abbreviation g for glycine a for ln and v for valen i four i solution l for leucine so as i say our h is the r group of glycine and ch3 is the r group of elenin and ch ch3 and ch3 is for valine okay all right guys now acidic we have two coh groups glutamate and aspartate this is the one letter e and d because they have been used for ln basic we have a lysine and arginine l have been used for leucine so it's k arginine are sulfur have one s right one sulfide cysteine cysteine and methanol in alcoholic we have serene and threonine with one o h group and in aromatic we have aromatic rings we have phenylalanine tryptophan and tyrosine and in the heterocyclic we have proline hydroxyproline and histidine fine guys okay now let's talk about the classification on the basis of polarity now all those amino acid for example your neutral amino acid and your methionine they do not have any charge and any polarity in them so they are usually considered under under the category of non-polar amino acid they are under the category of non-polar amino acid okay now let's talk about polar ones so in polar ones there can be amino acid which are charged and which are uncharged okay so here we have the one which are uncharged that means polarity will be there positive and negative having positive and negative charge is what is polar but if any of them charge is dominating like two we have two positive charge and one negative charge so it will be charged polar because it have more positively charged it will be basic it will be basic so arginine and lysine they come under the polar charged one which charges dominating the for example two positive charge are dominating only one negative is there now negatively charged for example two negative are there only one positive is there so this one is negatively charged and polar so here we have aspartate and glutamate in this one we also have histidine aromatic are also non-polar ones aromatic are also non-polar ones so we can also classify them according to the polarity whether they have it or not upper ones they don't have polarity lower once they have now in polarity do we have any dominating charts like in this one we do not have any dominating charge we have this situation here we have one dominating positive charge here we have one dominating negative charge all right okay now let's classification is on the basis of how important are they to your body so one are essential another are like semi-essential third are non-essential amino acid so anything that is formed inside your house or you already have in your house so you are not much yeah you don't care about that thing right but anything that you do not get easily you care about that thing a lot right for example you do not uh or your mother do not cook a pizza every day okay and the pizza that is you know completely like fresh from oven with lot of cheese and all just like it they they serve in the market so that's quite essential for you that's important for you and you crave for that so that's not uh usually formed in your or you know they're not cooked in your house so for for you that's very essential but if i talk about sambar or dal or chawal roti right uh these rice and so so these things are cooked every day so if you are like bored yeah i don't care they're not that essential right so anything that you do not have and your body does not produce that is essential for you so you need to take it from your diet so all these amino acids are essential amino acid these are not produced in your body these are not produced in our body so we have to take it from external diet what is this lysin leucine isoleucine valine phenylalanine methionine tryptophan and threonine right so here you can learn it uh like live life in vegas please must try t how can you learn it i have a mnemonic for this live life in vegas please must try t okay in semi-essential these are the one that is produced in your body but in less quantity or for example at certain period of time they are formed another they are not for example in children they are not formed in adult they may form or we can say they are formed in pregnancy but they are seems to be in low quantity so if that are semi-essential arginine and histidine they are not formed in sufficient amount formed in sufficient amount next non-essential they are always produced in a body whatever other 10 amino acids are left they all are non-essential okay so that's how essential some essential and non-essential amino acids are let's move further guys and talk about okay proteins let's talk about proteins so if we talk about proteins proteins are what they're polymers polymers of amino acid but they're not homopolymers they are heteropolymers they are heteropolymers of amino acid of amino acid how heteropolymer like this is a1 this is a2 a3 all amino acids are different this might be alanine this might be glycine this might it might be lyson so it's a chain of a number of amino acids okay second thing to note here is that which is the most abundant protein in animals most abundant protein in animals that's collagen most abundant protein in plants that is rubisco the one you use in photosynthesis all right okay so let's see what is the various structure of a protein so protein is present in four forms of structure from simple to complex the simplest one is primary structure a more complex secondary then a more complex tertiary most complex quaternary structure fine so we'll start with the primary structure one so primary structure is like all the amino acids are joined in this chain like fashion all the amino acids they are joined in a chain like fashion for example this is one amino acid i'm talking about primary structure first not to get confused guys let me just write it neatly first we have primary structure so in primary structure we have like this amino acid one amino acid and this is the another amino acid okay now they're going to join let's see how do they form a bond let's see how do they form a bond so as you can see here in biomolecules whenever you have to form a bond whenever whether it's carbohydrates it's protein it's a lipid you have to remove water you have to remove water so here you will remove water like this and what will be formed here co nh ch r coh so this will be formed so this bond is known as peptide bond this bond is known as peptide bond so peptide bond is a bond which is present in between the amino acid this end have free coh group this is a c terminal this is having the uh free nh2 group so this is the n terminal so n terminal amino acid is always considered the first amino acid this is always considered the second or the last one and you always read from n to c because we need to read the sequence of amino acid right now so if i do more twisting and coiling of the structure i can get the secondary structure what structure can i get secondary so the secondary structure is of two types it is formed by the more twisting and bending of the primary structure one is alpha helical and another is beta pleated so when we are doing some twisting or bending during that time you need certain other bonds to stabilize that structure if i'm doing bending or something i will be needing energy so for bending or twisting i need certain bonds so like here i have this right handed helix alpha helical structures or will always show right handed helix okay now here somewhere the coo group must be hanging from co h and somewhere here n h must be hanging so o and h can easily form hydrogen bonds so hydrogen bonds are the bonds that are responsible for stabilizing secondary structure it's a kind of a 2d structure or two dimensional structure you can find this in the myosin in the myosin you can find this in the tropomyosin you can find this in the actin and you can also find the structure in the collagen so all these they show alpha helical structure then we have beta plated beta plated structure is present in the form of plates like that it's present in the form of plates one plate above the another this is n-terminal this is c terminal like right like this and in between two plates will be present hydrogen bonds so what is what are these bonds hydrogen bonds you find this in the keratin protein in keratin protein okay the one in the hair and nails so that's the secondary structure let's talk about the tertiary structure tertiary structure is quite important tertiary structure is formed by further twisting and bending of secondary structure the only thing is that one structure is leading to the bending and forming the another one primary showed the bonding form secondary secondary did the bending form tertiary and tertiary is present in the form of a woolen ball you know own kagola it's just like that okay this is just like that so you'll see the structure in the enzymes where you find it enzyme and this is a kind of a 3d structure and very important for biological functions for example i say this tertiary protein structure this tertiary protein structure is seen in enzyme if the tertiary protein structure is destroyed in an enzyme enzyme will no longer be functional it will not be doing its biological function of catalysis right now what are the bonds that are important or that stabilize this tertiary structure these bonds can be ionic bond known as electrostatic it can be hydrogen bond it can be wonderful forces okay wander wall forces it can be the sulphide bond disulfide bond disulfide bond is formed between two cysteine molecules or two cysteine amino acid okay ah covalent bond which is a kind of a covalent bond ok and it can't be it can be hydrophobic interactions as well so all these structures or bonds can stabilize the tertiary structure and you can see that in inside now let's talk about the last structure which is a quaternary structure now whenever you have more than one polypeptide chain you know what is a peptide chain so in the primary structure this thing that we have formed is a peptide when you will join a number of amino acid that will become a polypeptide that will become a polypeptide okay when you will join a number of amino acid like this this will become a polypeptide okay if i say i have used only two amino acid this structure is a dipeptide this is a dipeptide when this polypeptide chain get twisted and bended it will form the secondary and tertiary structure but when number of polypeptide chains are involved then it will form a quaternary structure it will form a quaternary structure as you can see this is one tertiary structure this is the one structure of protein tertiary structure with one polypeptide chain imagine this is one subunit and i have such kind of these subunit in the number four or i have total four subunits like this now they need to be together and they will be forming bonds and one type of a structure is formed that is a quaternary structure let me elaborate it more so quaternary structure is formed when you have more than one polypeptide chain poly peptide chain okay let me give you an example for example this is primary structure with a polypeptide chain now this causes twisting and bending it becomes alpha structure alpha helical or secondary structure now more twisting and banding occurs it becomes tertiary structure this is secondary structure this is primary this is how i write primary secondary industry when such kind of four units are joined like this then it will become tertiary structure as a best example of this is hemoglobin so hemoglobin is made up of two alpha and two beta chains right imagine this is alpha alpha beta beta alpha one alpha two beta one beta two chain right so this is how the hemoglobin shows the quaternary structure all right let's read the ncrt we'll start from here guys you can open the ncrt page number around 149 the sequence of amino acid that is the positional information in a protein which is first amino acid which is second and so on is called primary structure of a protein a protein is imagined as a line the left and represents by the first amino acid and the right end represented by the last amino acid this is what we have done right like this first amino acid last amino acid so primary is in the form of line and whenever you have to check which is where does the amino acid is present or what's the sequence of amino acid you will always check primary structure of a protein the first amino acid is also called n-terminal amino acid the last amino acid is called c-terminal you know now why a protein thread does not exist throughout as extended rigid rot so it can never be present in such manner you are you have to coil it up for example if you will coil it becomes alpha helical then it will be your kind of myosin and tropomyosin if you more twist it it will become tertiary structures so you will never find the amino acid in this proteins in this structure you will hardly find it in the structure mostly you will find them in a functional form then it might be secondary tertiary or quaternary structure all right of course only some portion of the protein thread are arranged in the form of helix in protein only right-handed helices are observed on the regions of the protein thread are folded into other forms in what is called secondary structure in addition the long protein chain is also folded upon itself like a hollow woolen ball giving rise to tertiary structure this gives a three dimensional view of a protein so which one is a 3d structure tertiary which is a 2d secondary tertiary structure is absolutely necessary for the many biological activities of protein some proteins are assembly of more than one polypeptide or subunit the manner in which these individual folded polypeptides or subunits are arranged with respect to each other is the architecture of a protein otherwise called quaternary structure so in quaternary structure we have like hemoglobin with four subunit hence two subunit of alpha type and two of beta type constitute the hemoglobin fine now these were the structure let's talk about these functions of protein first function it act as like collagen or we can say collagen is a protein it's present as in the form of fibers in the intracellular ground substance or we can say intercellular metrics we have done it in connective tissue trypsin it acts as an enzyme and it breaks protein insulin is hormone antibody fights infection receptors they receive something we have done in the hormones we have done in the sensory receptors glute4 this is the one might you will not know glut4 glute glu means glucose t means transporter so these are certain proteins which are present on these cells for example on the liver cell and they will lead to the transport of glucose so they are glucose transporters all right guys so that's about your uh an amino acid let's talk about certain questions hydroxy methyl is the r group in the amino acid hydroxy means o h methyl ch2 so this group is present in which amino acid for example you do not know the structure of every amino acid but you have learned this classification that i wrote according to structure and i have told you oh will always be present in alcoholic amino acid and there are only two amino acids in alcoholic one is serene another is threonine okay now glycine is neutral it will have a ch2 or h as a group alanine is also neutral as part it is acidic it will be having extra coh serene is the alcoholic one answer three even if you cannot learn the entire structure this is practically impossible you uh all you can do is to uh learn that chart that i've given according to structure classification okay next question which of the following is an essential amino acid arginine histidine glycine lysine very very simple question the only thing you have to do is here you can see we have done arginine and histidine they are semi-essential okay live life in vegas learn this one lysin is essential one do you see any glycine here no i can't see that's non-essential this is the only thing that you need to understand right guys so which one will be the essential here live life in vegas 4. these are semi-essential this one is non-essential choose an incorrect statement from the following amino acids are substituted methane true okay we have to find the incorrect one next in proteins only right-handed helices are absorbed true tertiary structure of protein is absolutely necessary for the many biological function true in polypeptide or a protein amino acids are linked by a peptide bond very true which is formed when the carboxyl group reacts with the amino group this is also true but of the different amino acid not of the same amino acid see only one word changes the entire sentence and that you need to read carefully so answer is four this is incorrect hydroxy methyl okay that's a wrong question i'm really sorry for that so let's now get started with the lipids so now let's get started with the lipids so now what are lipids so you must have heard of fats so lipids are generally you're obviously because the carbon containing compound that's why we are studying them in the biomolecules so these are also made up of carbon hydrogen and oxygen but it has less oxygen than carbohydrates it has or it contains less oxygen than carbohydrates so your lipids they are insoluble in water you have you ever done that if you will dissolve oil in the water if you will you will dissolve oil in the water it will not get dissolved rather it will come up on the surface so this tells us that they are not soluble in water they are not soluble in water but they are soluble in they are soluble in some organic solvents fine now what is basically a lipid a lipid can be made up of a fatty acid what is a fatty acid fatty acid is the acid which have r group with it or it has a long chain of carbon and to that one cooh is attached like i say it has like 17 carbon chain and then one coh is attached that's your fatty acid okay or it can also be the ester ester of fatty acid and alcohol in this case the alcohol is usually your glycerol alcohol is usually your glycerol so a a single fatty acid can also be considered as a lipid or fatty acid with uh the which is uh which has done you know sterification with alcohol is can also be considered as a lipid now let's see what are these fatty acids so fatty acids are like a long chain have long chain of carbon and coh attached to it like here you can see this is one fatty acid known as palmitic acid so it has a long chain of carbon as you can see here it has a long chain of carbon this is its r group and one coh is attached to it as you can if you can count how many carbons does this fatty acid have the name of fatty acid is palmitic acid the total number of carbon is 14 15 and 16 so it has total 16 carbons okay now fatty acids are of two type one is saturated another is unsaturated so whenever you think of learning the saturated and unsaturated imagine uh you know two two lipids here one for saturated imagine ghee right you know what is a ghee right and uh imagine here about oils like your refined oil or something like any oil like a mustard oil okay so these saturated fatty acids are the one which do not have a double bond so if i say palmitic acid is a saturated fatty acid so this one can you see here any double bonds no only single bonds are present whereas in the unsaturated double bonds are present if you know when there is winter the ghee gets solidified he gets solidified why because ghee have high melting point it have high melting point and this one have low melting point so that's why it is a high melting point you need to give it more heat and then you can you know liquid liquefy it and here you you don't need to give a lot of heat they have low melting point so they will appear as a liquid even at room temperature so what are the example we have palmitic acid in saturated stearic acid and arachidic acid palmitic acid have 16 carbons steric acid have 18 carbons and arycatic acid have 20 carbons on the other hand in unsaturated we have 18 carbons 18 carbons 18. olic linoleic linolenic all have 18 carbons then what's the difference the difference is in the number of the double bonds so allic have only one double bond linoleic have two double bonds linolenic have three double bonds and arachidonic is having like 20 carbons and it have four double bonds so all those which have number of double bonds you also consider them under pufa so the one which have two three and four double bonds linoleic linolenic and arigatonic all these comes under the category of pufa that means poly poly means many unsaturated means double bond fatty acid so they have number of double bonds so that's why you call them as pufa polyunsaturated fatty acid and this one is mufa what is mufa mono unsaturated fatty acid because it has only one double bond so if you'll see any uh whenever you eat something okay so the things you buy from outside it contains or it's present in the form of packets right for example you bought a packet of chips or you bought a packet of some bhooji or something right so behind that there is a rule that if if anyone is uh selling a product which is eatable especially the proprietary food that means a ready-made food they need to mention its nutritional information even if on the packet of maggie nutritional information is written behind it so there you will see the muffin puff are also written and that is important and that tells about the calories also so whenever you are eating something do check the nutritional information if it is rich in vitamins rich in pufa it is rich in minerals eat that thing and if it has it does not have all those things it has only like carbohydrates and bad fats just avoid eating all those stuffs right and also check for the preservatives especially um when you have a lot of preservatives and food avoid having that food so that's why it is said now always your mother says always eat things that are you know cooked in home and so on so if you have seen this um eating outside has been such a you know trend in our generation more it was not in more than our father mother or grandmother's you know time they don't eat from outside they didn't eat from outside they used to they cook food at home and they used to eat at home and that's why they were more healthier and have a lot of power and strength than us right okay anyways let's um talk about the classification now so if i classify the lipids there are like around three types of lipid one are simple lipids second are conjugated lipids or compound lipids and the third is derived lipid third is derived lipid okay so here in the first one that is your simple lipids simple lipids are just made up of fatty acid plus alcohol okay and we have three types of lipids here first we have true fats second we have waxes and then cute in subarin in case of plants it's present in plants so we'll not be discussing that in detail because i teach is zoology now conjugated or compound they have fatty acid plus alcohol with them and along with the alcohol they have one group attached to it if it if if this group is phosphate so here the lipid will not be will be known as phospholipid okay and then we have the derived one these are not the asterisk of fatty acid and alcohol they are the modified version of fatty acid so here we have the two example one is cholesterol which comes into the category of steroids so basically don't we'll write steroids here which have one example cholesterol and second prostaglandins okay so these are the things that we'll be discussing in detail the most detail will be discussed of true fats fatty acid and steroids okay all right so let's get started with the simple lipids so as i've told you simple lipids are made up of uh they are the esters of fatty acid and alcohol so here the first one we have is true fat in true fats or the true fats are basically the esters of fatty acid plus alcohol and what alcohol is this glycerol so how does a glycerol looks like glycerol is chemically tri hydroxy propane so if i'm saying it is propane how many carbons that will be having three carbons so this is how it will be having three carbons okay so here ch2oh choh and ch2oh this is one molecule of glycerol this is one molecule of glycerol you got it right this is one molecule of glycerol and as it has three alcohol oh groups so that's why you call it as trihydroxy propane now these two will undergo esterification and they will form your fats let's see how do they form the fat so here what happened guys here we have a glycerol molecule like this and glycerol molecule have 3oh so what do you think how many fatty acids can do the esterification with this one molecule of glycerol this is one glycerol what do you think how many fatty acids can undergoes terrification with this three why because it has three o h right for example i added one r one that means first fatty acid now this first fatty acid will do the esterification process with the o h of the first one okay so let's see how it this will go on so here c h2 o c o o and r one this is how the first fatty acid will form ester with the first oh and now this structure will no more be known as glycerol rather you will call it as monoglyceride what will you call it as you will call it as monoglyceride now let's add now let's add one more fatty acid now this fatty acid will do or est will form ester bond with that now how the extra bond is formed for example this is o h this is o h you just need to remove water as i've told you always remove water in biomolecules to form a bond whether it is a glycosidic bond whether it is a peptide bond or whether it is the ester bond now here you can see easily the bond is going to be made the first one is already forming the ester bond with the first fatty acid and this one will form the ester bond with the second one and now the structure is no more known as monoglyceride mono was the the reason because it has only one ester bond now because it has form two ester bond this will be known as diglyceride now when the diglyceride is now going to react with the third fatty acid now what will be formed let's see now the third third carbon third one will also form ester bond with the third o h right here here now the structure will be known as most of you must have guessed it as well triglyceride so if someone asks you if someone asks you how many fatty acids do we need to make a triglyceride you will say three and how many glycerol do you need to make one triglyceride just one glycerol the same glycerol is going on you don't need to take number of glycerol because one glycerol have three oh right and to one glycerol three fatty acids can be attached again now if someone asks you how many glycerol do you need to make one diglyceride again one and how many fatty acids do you need to make one diglyceride you will say two again how many glycerol do you need to make one monoglycerite you will say one but how many fatty acids do you need to make one monoglyceride again one fatty acid so this is a very common question that can be asked in the exam even in this exam a lot of questions have been asked from fatty acid you won't believe there was a complete statement based question and that contained around all the paragraph of the ncrt or flippets imagine so they have asked about this uh they have mentioned one sentence that was what it is insoluble in water but soluble in in inorganic solvent second statement was on the saturated and unsaturated one about the melting point there was also another statement of palmitic acid and there was a statement from this one also monoglyceride diagnostic also right so since uh you sometimes you feel that from one topic only one question can be asked that's true but it may contain the entire aspect of that topic right so always always read each and every line of ncrt very carefully okay anyways guys let's move forward let's talk about the compound lipids so as uh you know about compound lipids we are going to discuss only one in detail as i've already mentioned so here we are going to talk about phospholipid so in the phospholipid what phospholipid is made up of since it's a lipid definitely it will be containing a fatty acid and a glycerol that's why it's a true lipid right uh sorry that's why it's a lipid fatty acid plus glycerol will definitely be there along with that a phosphate group will be there a phosphate group will be there but there are certain structure who have this this structure which contains fatty acid glycerol and phosphate but along with that they might can also contain an extra group like sometime the nitrogenous group and sometimes a nitrogenous group can also be present let me give you an example of a phospholipid so if you have ah read the that chapter cell and cell membrane in cell membrane we have a phospholipid right and you know that in phospholipid one molecule is hydrophobic and other is hydrophilic do you know that for example if this is uh the portion and this is the chain portion this one is hydrophobic and this one is hydrophilic so same uh same the phospholipid we are talking about this one is present in the cell membranes okay so here the example that i'm going to discuss with you is lecithin so lecithin we have already discussed this also in the chapter breathing and exchange of gases lecithin is present in the cell membrane and also it prevents collapse of alveoli prevents collapse of alveoli because it acts as surfactant and what's a function of surfactant surfactant reduces surface tension it reduces surface tension and prevents the collapse now this is a structure of lecithin so lecithin contains a glycerol this is very true we have glycerol it contains fatty acid let me mark it also yes we do have fatty acids to fatty acid now third is o h or the third o h okay this first o h is conjugated with fatty acid right with the r group second one is also making ester bond with the uh another fatty acid so first two o h are making normal ester bonds with the normal fatty acid with long r chains now the third one is also forming ester bond but here this is not a normal fatty acid rather this is phosphoric acid this is phosphoric acid so phosphoric acid is also the acid and whenever o h and or we can say whenever alcohol and acid they form bond that always will be the ester bond now this uh you know acid can be different it can be a fatty acid it can be a phosphoric acid as well so here the third which is forming the phosphoester bond okay so this one is a phosphate bond form but the bond is the ester bond only so this is the entire structure of a phospholipid now because this is a structure which is lecithin it has an extra group it has an extra group and the name of this nitrogenous group is choline so choline is a nitrogenous group present in the lecithin right so this entire structure this entire structure is of a phospholipid which is attached to the extra group which is the nitrogenous group and this is how lecithin is so important and this is how its structure looks like so what kind of a question can be asked in the exam they might give you this uh structure you have to identify it okay all right so that's about your compound lipid let's talk about the derived one in derived lipid the first one that we have is steroids steroids okay so steroids are not the esters of fatty acid and alcohol rather they are the modified fatty acids right they're formed by the modification of fatty acid they are modified fatty acid so steroid is a very large glass steroid is a very large class under steel oil the most common is sterols the most common steroid is sterols sterols are of different kinds like sterols can be found in animals they can be found in plants and they can be found in the fungus as well right so we are not concerned with fungus and plants here we are concerned with the animals so in animals the sterol that we have is cholesterol so if you can see clearly the cholesterol word has sterol in it it has a sterol in it the cholesterol structure looks little like that so it contains four rings out of this three rings are hexagonal and fourth is a pentagonal ring here you have o h which can be used for a sterification where sometimes it needs to get conjugated with the fatty acid right so yes it do can but the entire structure it's not a you know it's not a kind of another alcohol okay so it's basically the modification of fatty acid only so here we have a long chain also of carbons so what's the use of cholesterol in your body now you must be thinking no no ma'am this is bad it causes us diseases the high amount of cholesterol cause you disease or you know cholesterol can never be transported alone they are always transported with the help of lipoproteins if those lipoproteins they are not sufficient in our body then the cholesterol can deposit in your tissues for example if i say there is a person who needs to go from one place to another and there is a long road and that road is uh empty and um there is no light and nothing it's it's in the forest if the uh any transport or like car or cab the with which the person wants to you know uh move or the person wants to relocate so if that car or cab is not available the person has to roam around the roads and maybe the person will you know forget the path and get lost somewhere so that person is basically like cholesterol and that car or cab are protein so proteins are present in sufficient amount that person can be easily transported from one place to another but if that car or cab or that proteins are not available so cholesterol will be deposited in some areas where it is not needed okay now so this cholesterol is present in your cell membrane guys where it is present in the cell membrane it's a very important component of cell membrane and this cholesterol is also used in the formation of formation of number of substances like steroid hormones estrogen progesterone testosterone all these are formed from this also the formation of bile in the liver and vitamin d so it also act as a precursor of vitamin d cholesterol right so cholesterol is uh you know performing these much function so this can also be act as uh like it act as a fat also in your body okay can be converted into fat so these are some of the what you say the uh you know role of cholesterol in animals okay so these are not always bad they can be good also now let's uh talk about the prostaglandins okay so green let's talk about the prostaglandins what are prostaglandins are also modifications of fatty acid so they're also modified fatty acid these prostaglandins they are abundant or abundantly formed during menstruation and punctuation what is parturation guys delivery of baby so they are abundantly formed there and they causes pain plus contraction of muscles so whenever a female undergo menstruation her muscles contract a little due to prostaglandins and the layer endometrium which is the innermost layer of the uterus it comes out also that's why the female also suffer from pain and craps so whenever there is inflammation you also get pain so wherever in your body you get the pain prostaglandin is the one that causes it okay so that's about the prostaglandin this is also your one of our derived [Music] lipid let's solve this question dash has 16 carbons including carboxyl carbon simple palmitic acid how many carbons are there in the palmitic acid 16 including the carboxyl carbon what is carboxyl carbon coh if it would it would have written excluding carboxyl carbon then it would again be palmitic acid and number should be written 15 okay all right next lecithin is a glycolipid phosphorupit sterol or simple lip but it's not a simple repeat in simple lipid we have true lipids waxes right in store stir all we have cholesterol and glycolipid we we have you know fatty acid plus alcohol plus carbohydrate these are also present in your cell membrane so this is a kind of phospholipid so answer to this question will be two next identify the structure and find the correct statement first triglyceride made up of three glycerol and three fatty acid diglyceride made up of one cholesterol and three fatty acid triglyceride made up of one glycerol and three fatty acid triglyceride made up of one glycerol and one fatty acid identify first of all it's glycerol for sure one fatty acid second fatty acid and third all three ester bonds have been formed with 3oh of glycerol that means it's a triglyceride so triglyceride all right triglyceride triglyceride triglyceride this one already out how many glycerol guys one glycerol and how many fatty acid three so answer to this question will be three right next let's talk about nucleic acid now what a nucleic acid nucleic acids are the heteropolymer hetero means they will be different types of monomers right they are the heteropolymers of of nucleotides the heteropolymers of nucleotides so you uh must be must have heard about dna or rna yes so that dna and rna they are nucleic acid they are nucleic acid fine now what are nucleotides what are nucleotides nucleotides are made up of sugar plus phosphate and with sugar there is one more thing that is attached which is nitrogenous base nitrogenous base plus sugar they are collectively known as nucleoside so you can also say nucleotide is made up of nucleoside plus phosphate you can also say nucleotide is made up of nitrogenous base blood sugar now what sugar is used in the formation of nucleotide glucose ribose a lot of sugars are there right and what a nitrogenous space and phosphate you already know let's talk about that so first of all the sugar the sugars used are of two types the sugars used are of two type can you identify these sugars no so this one is your ribose and this one is your deoxyribose now how does mam knows about this because ma'am have done a lot of study no not like that so even you know about that what i'm talking about you can see on the second carbon oh is absent but here oh is present so the deoxyribose was a derived monosaccharide that was formed from the um ribose and how does it form from the ribose only one difference is there it loses its oxygen here on second carbon so deoxyribose sugar is always found in the dna and this one is always found in the rna now you have this phosphate ion and phosphoric acid these are also used in the formation of the nucleotide now the third thing that you must have not heard about anywhere so that are your nitrogenous bases nitrogenous base so this nitrogenous base nitrogenous base are what their heterocyclic compound what are heterocyclic we have done this in amino acid as well heterocyclic compounds are the compounds which contains a ring heterocyclic ring which is not just made up of carbon but it might contain nitrogen as well so you can see here nitrogen is present in the ring you can see nitrogen is present in the ring so we have classified these heterocyclic compounds into two categories one is purine and another is pyramidin one is purine another is pyramidin what's the difference the purine are double cyclic compounds that means it will contain two rings so the one that you can see above this structure it's of for purine okay and pyrimidines are always single cyclic they are made up of only single ring so purines are of two type one is adenine the structure of adenine is already given there and another is guanine so you use one letter abbreviation a for adenine g for guanine similarly in pyramidin we have cytosine which is which have an abbreviation c then we have thymine which have abbreviation t and we have uracil with you okay here there is a thing adenine guanine cytosine these all three can be present in dna as well as in rna but thymine is only found in dna then in place of thymine rna contains uracil and uracil can only be found in your rna the reason is because uracil is compatible with the ribose sugar and ribose is present in rna and thymine is compatible with the deoxyribose sugar so that's why it is present in the dna okay all right so now let's make a nucleotide as i've told you it is made up of one sugar imagine this is your sugar all right take it the ribose imagine this sugar this one is your ribose sugar okay now on first carbon on first carbon a glycosidic bond has been formed between the nitrogenous base and here uh your we say on first carbon always on the first carbon of your ribose sugar or deoxyribose sugar nitrogenous base will be present so how it is attached to the sugar by producing one bond and the name of the bond is glycosidic bond now the fifth carbon is this one one two three four five now with the fifth carbon the phosphoric acid will try to produce a bond again what you have to do in the biomolecules you just have to remove water let's remove water h2o and now a bond is formed here and what's the name of the bond the name of the bond is not the james bond the name of the bond is phosphor ester bond so most of you confuse it with phosphodiester that's different so between a sugar and phosphate of the same nucleotide this is one nucleotide same nucleotide phosphor ester bond is formed between sugar and nitrogenous base glycosidic bond is formed now we have said that your dna is a nucleic acid and nucleic acid is a heteropolymer of nucleotide now let's see how the dna it looks like okay but before that let's name the nucleotides first okay so you can see this one and this is important so whenever we are using the nitrogenous base as adenine what will be the name of its nucleoside you will say adenosine similarly if i'm using guanine as nitrogenous space what will be its nucleoside known as guanosin for example if someone asks you a question what are the components of guanosin then what will you say you will process in your brain guanosin is a nucleoside and nucleoside contains sugar and nitrogenous base okay now what if i am making nucleotide and adding phosphate because this one will contain nitrogenous base plus sugar plus phosphate this one will contain nitrogenous base plus sugar now because it has formed bond with an acid it will be known as an acid so this will be adenylic acid and this will be guanilic acid similarly here cytosin now cytosine is a pyrimidine cytosine is a pyramidin so i will be using word din din and in in pyrimidines because all these three are pyrimidines so i will be using word in here in the their nucleoside cytosin cited in thymine thymidine uracil uridine now add acid cytodilic acid thymidalic acid and uridylic acid now if someone asks you uh what are the components of thymidalic acid what will you say nitrogenous base which is thymine and sugar and plus phosphate will be there okay so this is how you can solve the questions of nucleotides let's talk about a nucleic acid which whose name is dna what's the full form of dna deoxy ribo because the deoxyribose sugar is used deoxyribo nuclear nucleic acid right deoxy ribonucleic acid okay now the model to explain dna was given by watson and crick so we are going to discuss the watson and crick model of dna so according to their model the dna is the dna is double stranded it is double stranded and helical but anti parallel what is anti parallel two strands will be moving in the opposite direction now let's see and both the strands are you know they are helical or they are revolving around one common axis for example let's make this a common axis okay and they say there is one strand like this and now there is a another strand like this another strand like this both the strands both these strands okay let me just make it more nicely for you all right now let's erase these okay so these are two different strands and it's helical as you can see it's helical as you can see okay so two strands they are helical two strands are helical and they're anti-parallel how we have marked them like this is the 5 prime end this is the 3 prime end so this one will be the 3 prime end of this one and this is a 5 prime end of this one and you always read from 5 prime to 3 prime this is what is a rule how it is anti parallel we always read from 5 prime to 3 prime end so 1 is in the direction of 5 prime to 3 prime and another one is in the direction of again in the opposite so this is how they are anti parallel and this one turn is of 360 degree it is of 360 degree okay whenever i am trying to do something perfect now it always uh get blunder and i really don't like the structure i have drawn see i have re i don't really like the structure i've drawn but i think you can understand so here this is one turn okay guys this one turn is of 360 degree how 180 180 okay i'm not satisfied let me draw it again now you must be thinking man what are you doing it's okay ma'am don't worry okay now it's little better okay now this one turn is of 360 degree this one turn is off 360 degree this is one turn one turn is of 360 degree now how much uh uh is the length of the turn how much is the length of a turn it is 34 m strong 34 i'm strong okay now if i say in one turn there are present total 10 pairs total 10 pairs of your nitrogenous base or basically the nucleic acid for example if i say so this is how these are present um 1 2 3 4 5 6 7 8 9 and 10. so if i say 10 pairs of your nitrogenous bases are present in this manner so this one is here like that okay so if i say one turn contains 10 base pairs bb means base pairs so how much is a dis distance how much is a distance between two base pair how much is the distance between two base pair and that is 34 divided by 10 that is 3.4 am strong so 3.4 armstrong is the distance between two base pair distance between two base pair so at every ascent there will be a distance covered of 3.4 amp strength right and during every ascent what is or at what angle every nucleotide is taking a turn or what angle does it is taking turns so that angle will also be of 36 degree so 36 degree is one turn okay so each nucleotide is taking a turn of 36 degrees all right now between two strand there is a distance of like for example how much is the distance in between these two distance between two strands is 20 am strong is 20 amp strong fine now another thing to note out note here is that always always in front of adenine there will be thymine always in front of guanine there will be cytosine for example if this is adenine in front of this always there will be thymine and they will be stabilizing the structure of dna by producing two hydrogen bond between them and in front of go on in there will be cytosine and they will be producing three hydrogen bond to to stabilize the structure of dna right so here always it will produce two hydrogen bond it will be producing three hydrogen bond i'm writing that in practice now why not adenine have guanine in front of it or why cytosine don't have thymine in front of it i'll explain you the reason is adenine and guanine both are double cyclic if i keep adenine in front of guanine both will be double cyclic they will be heavier in their molecular weight and they will not be compatible and they cannot accommodate so we want that the thickness remain the same okay for example i added here adenine is also double cyclic guanine is also double cyclic there and here i added thymine and cytosine okay so thymine and cytosine they are single cyclic so here the distance between both the uh these nucleotide will be less but here the distance will be more so that will become an uneven structure but we want a similar or nature wanted more stability so for stability we want the same amount of distance between all the nitrogenous spaces okay so that's why there is 20 amp strong distance this is double cyclic this is double cyclic this is single this is single simple okay all right now let's draw a molecular structure so if you'll see uh what the back bone is made up of for example this was the entire structure all right so these were the um nitrogenous spaces these are nitrogenous bases like adenine these were nucleotides and these are nitrogenous bases you can see nitrogenous bases they are hydrophobic and they are present in the inside of the structure whereas the backbone is always made up of sugar and phosphate right remember this one thing the nitrogenous bases they are hydrophobic that means they are they have fear of water so they are present towards inside right whereas the backbone of the entire structure is made up of sugar phosphate now we have to see how the sugar phosphate is arranged for that we need to understand the molecular structure so for example this is one nucleotide one sugar because this is dna what will be the sugar deoxyribose so here you have oh here here you don't have any o h this is first carbon and this is carrying for example adenine okay this was the fifth carbon which is uh forming the phosphor extra bond with the phosphate this is how one nucleotide is right just see it carefully no doubt i guess there will be no doubt if you know the structure of a nucleic acid and nucleotide basically now similar kind of a nucleotide will be present here also as i have told you the nucleic acid are the heteropolymer they are the heteropolymer of nucleotide so we need a number of nucleotide and then nucleotide will be different why some may contain adenine some may contain thymine some may contain guanine okay now here i have used adenine let's use guan in here okay now on this one we have again a phosphate attached which no h and here we have o h all right now this is a pick so listen to me very carefully this is the one strand this is the one strand this is uh you know we say it's double helical there are two strand this is just one strand now let's see how two nucleotides are attached this is the first carbon this is second third fourth fifth first third fifth now first is already attached with the glycosidic bond so you don't have to do anything with that now the third one the third carbon or the o h present at the third carbon of one nucleotide or the first nucleotide will form ester bond with the phosphate of the subsequent or the second nucleotide car oh on the third carbon or first nucleotide will be forming ester bond with the phosphate of the another or second nucleotide so you just need to remove water let's remove water so when you will remove water here what will be formed guys what will be formed an ester bond will be formed because this was oh and this one is acid so it will remove water and will form a bond now this bond is not phosphor ester bond rather this is the second ester bond formed because first bond is this one first phosphorous bond is this one first first first bond is this one so this one will be second phosphoresctor bond so you will name it as phosphodies bond you will name it as phosphodiester bond okay so phosphodiester bond is the bond which is formed between two nucleotides this is first nucleotide this is second nucleotide and helps in maintaining the backbone this is a very common question asked phosphodiester bond is formed between the sugar and phosphate of same nucleotide or different of the different nucleotide now the fifth carbon here is containing phosphate and this is not forming any ester bond with the subsequent nucleotide because there is no subsequent nucleotide okay here this one is free it cannot form any bond because there is no nucleotide above this so this end has a free phosphate at five uh at the fifth carbon so you call it as five prime end similarly because it does not have any other nucleotide below it so its third carbons o h is free and not forming any phosphodiester bond so this one will be three prime end and you always read from 5 prime to 3 prime now let's talk about the another strand of the dna and this one is an anti-parallel direction so it will be something like that here this is the first carbon with high mean this is the first okay first second third third have oh this is fourth and fifth have phosphate okay similarly there will be a nucleotide present below this like this and here the first carbon will be having cytosin because it is guanine and here there will be third oh and here's ch2 o o h o h fine again if i have to join these two nucleotide what i will be doing i will be removing water and again an ester bond is formed that is your phosphodiester bond phosphodiester bond now again let's uh mark their uh polarity here on the third one o h is free not forming any phosphodiester bond so this end will be the three prime end here phosphate is not forming any bond and this will be the five prime end and you always read from five prime to three prime okay so this is how their opposite stand adenine always form double hydrogen bond guanine always form triple hydrogen bond and any dna sample who have more go on into cytosine content as comparison to adenine and thymine content the dna is comparatively more stabilized okay all right guys so that's about the structure of a nucleic acid let's uh move further and talk about the another nucleic acid that is your rna now what's the difference between dna and rna the first of all full form ribonucleic acid and this one does not contain this one does not contain any first of all deoxyribose sugar it contains ribose sugar second it will not contain thymine it will be containing uracil as comparison to dna this is uh one standard or you can also say it's single stranded it is single stranded another point to note down here is that the rna as comparison to dna is little unstable there are three types of rna one is mrna second is r rna and third is trna now you must be wondering ma'am what's the full forms okay let's see m means messenger rna r means ribosomal rna and t means transfer rna you also call it as adapter so rna performs a very important function of uh protein synthesis okay all right so let's discuss the function then i'll show you how do they do it first of all messenger rna is the uh you know highly unstable and their number is very less and the most abundant out of all these three will be the rrna okay messenger rna is the one that is carrying the information genetic information from the dna for protein synthesis so this is the one that is coming out from the dna and contain message contains message or information or codons or codes of protein synthesis this is the one which is a site of protein synthesis because this is the one which will form ribosomes okay so this is the this is the site of protein synthesis and this one transfer rna it carries amino acid it carries amino acid all right let me give you um how does it happen for example this is your nucleus nucleus contains dna dna forms messenger rna mrna by a process known as transcription and this mrna contains genetic code for protein synthesis now this is ribosomal rna or ribosome and this will take up this mrna okay this is like rrna and this is mrna this contains the information for genetic code now how does how does protein form protein is a chain of amino acid so whenever for example if these are amino acid these amino acids they sit on these sites and they are joined to each other by formation of bones like this but there are there must be something that will bring these amino acid that will bring these amino acid so who or which rna bring the amino acid for example this is a trna so trna or adapted rn rna it will bring amino acids from the surrounding or cytoplasm and it will give the amino acid to the ribosome and ribosome will make chain of them reading this information it will because this information will tell which amino acid will uh be present first and we should be present next right so this contains that information and this is how the protein synthesis takes place this is just a vague information about protein synthesis the detail you will be doing in the class 12th okay all right so that's about nucleic acid guys let's solve some question for nucleic acid the building block is a very simple nucleotide answer one next the bond between the phosphate and hydroxyl group of a sugar in a nucleic acid is peptide ester hydrogen glycosidic very simple question tell me what bond is there between sugar and here phosphate what is this bond o h and phosphoric acid ester bond phosphorous bond you say it right this one is glycosidic with nitrogenous space identify the structure and find the correct statement first of all what see what is this this is a ribose sugar guys okay this is the ribose sugar this is the purine nitrogenous base this is phosphate attached so for sure this is a nucleotide so it's a nucleoside no it's a nucleotide true and the name is adenosine adenosine is the name of nucleoside with the nucleotide you always used acid okay it's a nucleotide and its name is adenylic acid it's a nitrogenous base at an end so answer to this question is three okay all right next the backbone in dna is formed by sugar and phosphate backbone so it's already written backbone with it the question is already done okay next next we're going to start with this dynamic state of body constituents the concept of metabolism so we are going to start with enzymes now so most of you what you do you generally skip these paragraphs don't you have to they are also important so here we are going to talk about metabolism first so in this chapter i have told you what is metabolism sum total of all the chemical reactions so here biomolecules are present in certain concentration expressed as moles or cells or moles per liter one of the greatest discovery ever made was the observation that all these biomolecules have a turnover the this means that they are constantly being changed into some other biomolecule and also made from some other biomolecule very true okay very simple uh thing that i'm trying to understand here trying to made you understand for example we have glucose you all know glucose should be present in a particular concentration in the blood if its concentration increases that can be a disease okay so this is first line says all biomolecules are present in a certain concentration very true second thing now this glucose will be converted into pyruvic acid pyruvic acid this pyruvic acid will later be converted into co2 and water and give you energy so this is what we say during glycolysis a number of steps takes place okay so here we say every bio molecule have a turnover what is turnover that means it is converted into one form and one form will be converted into another so for example this is a substrate enzyme will work and it will become the product and later on the product will then become a substrate and it will form other product so we say every biomolecule is not just sitting in your body it's constantly being converted into the another this is what turnover is this is what turnover is right so everything is present in two form the chemical reactions are present in two form they can be like linear reactions like that okay like glycolysis is a linear kind of reaction some reactions can be circular like a give rise to b give rise to c c rise to d and d form again a so they are like cyclical reaction okay so for example krebs cycle krebs cycle is the example of cyclical reaction so both type of reactions are going on in your body and they are constantly turning one things into the another and that's turn over it's turning one thing into the another now metabolic pathways are the pathways that are used in the metabolism okay so they can be of two type one is anabolic and another is catabolic pathway so anabolic pathway is a constructive pathway what pathway guys constructive that means it will be forming some things catabolic is the one the which is destructive pathway it will be destroying thumb some things it will be breaking something very simple like a lot of glucose will join to become glycogen and if the reverse takes place the glycogen breakdowns into glucose and glucose breaks down into pyruvic acid so everything is breaking down here to give energy that's a catabolic reaction again in the liver from acetic acid you can make cholesterol so here you are building things from monomers might be you will form polymers but here from polymers you are converting into monomers and monomers are later also destroyed so that's the catabolic pathway in catabolic pathway always energy is released energy is released and here energy is used because you are forming bond and here you are destroying bond and energy is always present in the bonds right and whenever you break the bond energy will be released all right so let's move further and talk about the living state what is a living state we always say something is living and for example our living cells are living how we say living state is a non-equilibrium steady state to be able to perform work if i'm talking about living state in terms of metabolism to prove something is living there are different types of concepts right when i'm when i'm talking about about metabolism i say that living state is an is in a non-equilibrium state steady state to be able to perform work first of all what is the study that everything is in the fixed concentration everything is in present in the form of fixed concentration non-equilibrium first of all what is equilibrium in equilibrium we say a gets converted into b and the process is reversible and when something is reversible we say that no work is done in equilibrium all right for example i'm giving you a very simple example in terms of biology sucrose is a sugar which is made up of glucose and fructose right so if i will use an enzyme which will break glycosidic bond between these two that is enzyme sucrase so sucrose when it is uh under the influence of enzyme sucrase it can be converted into glucose and fructose this is how it is breaking the bond okay now if i say the reversal takes place then the glucose and fructose will become sucrose again so that will be an equilibrium that would be equilibrium our body cannot afford equilibrium our body wants to be in non-equilibrium state because in non-equilibrium work is done work is done so here the work is done sucrose have been converted into glucose and fructose glucose will later on give the energy imagine if we would be in the equilibrium the reverse would have taken place there will be no glucose formation and you will not be able to produce energy or if i say in glycolysis the glucose forms pyruvic acid and later on again form glucose will pyruvic acid be destroyed to give you energy never you cannot you cannot live in equilibrium state so a living state is always non-equilibrium because in non-equilibrium work can be done and everything should be in the fixed concentration nothing should be higher nothing should be less okay all right so also you know that uh what's the concentration as i've given you given you an example glucose what is the amount of glucose in your blood 4.5 to 5 millimolar is a glucose concentration okay so it's always in that concentration it's less that means or more there can be certain disorders okay all right let's talk about enzymes what are your enzyme so enzymes are bio catalyst what are these bio catalysts catalysts are something that will increase the rate of a reaction what enzymes are made up of they are made up of proteins they are made up of proteins except certain enzymes like ribozymes which are made up of rna so rna sometimes attacked as uh you know a catalyst because it has a certain enzyme which can or it is basically its rna have a catalytic property like that of enzyme okay that's it now what structure of protein does enzyme exhibit it exhibit tertiary structure so you remember what's a tertiary structure a woolen ball like structure polypeptide chain it's you know wrapped around each other like a woolen ball so when it is wrapping around like that a small site is formed you call it as active site you call it as active site so this is the active site and two active site substrate binds substrate bind what is a substrate anything anything that has to be converted for example in the previous one i said sucrose uh in the presence of enzyme sucrose gets converted to glucose and fructose so these two are products sucrose is a substrate and so grace as you all know it this is an enzyme okay so this has to bind with the enzyme to do this reaction so how does it bind on where does it bind to the enzyme it will bind to this active site of the inside okay so now this is how it binds to the active site apart from the active site there is one more site present on the enzyme this is the allosteric site this is the allosteric site allosteric site okay let me just increase the font size yellow steric site allosteric site is the site to which usually inhibitor binds whenever you have to inhibit enzyme or you have to stop the function of enzyme at that time this site is used when and how we'll be talking about that in another part of this chapter okay now you must have heard of you must have heard of that there are certain inorganic catalyst present in chemistry have you heard of them there are one inorganic catalyst and then there are biocatalysts your enzyme now what's the difference between the two what's the difference there are also an organic catalyst first of all this one biocatalyst bio means living they are always used in living state in living organism these one are always used in non-living state the bio catalyst they are always made up of proteins they can be metals they can be metal lines also like palladium right platinum they can also act as the catalyst first of all these biocatalysts they are very specific in nature if such rays is an enzyme it will only convert sucrose it will not convert lactose right so they are very specific in function specific in function they are non-specific so platinum or palladium they can catalyze a number of different types of reaction second high temperature or at high temperature the structure can be destroyed why because they are made up of protein and when you give high temperature to protein protein gets denatured or it gets destroyed how does it get denatured its bonds will be destroyed okay so here at high temperature protein structure is destroyed and you call this as denaturation the bonds break and they can work at high temperature because they're metallic all right but there are certain exception here there are certain enzymes which can survive high temperature except thermophilic bacterias thermophilic bacterias are the bacterias that lives in hot springs you know what are hot springs usually in the mountain areas or near the volcanoes there are certain small ponds like structure or rivers which have very hot water in them they are hot springs and around that there is you know floor and fauna and that is you know the one which loves heat and they can survive heat so here there are certain bacterias thermophilic bacteria they can survive in hot springs why because they have certain enzymes that can work at that temperature around 96 degree celsius as well so that's an exception okay anyways let's talk about the chemical reaction now what are these chemical reactions so the chemical reactions chemical reaction you have heard a lot about them you must have heard a lot about them in the chemistry so they are of two types one are inorganic which you do in chemistry another are organic reaction so the one which you generally do in chemistry as well but most of them they belong to biology okay so so one such reaction in a body that's going on right now while you're studying is co2 is uh getting reacted with water and forming carbonic acid and then this will later on form the h-positive ion and hco3 negative ions that we do in the which we have already done this in the breathing and exchange of gases as well so here this reaction needs an enzyme because uh without enzyme the reactions they can be really very slow because the enzyme they increase the rate of reaction they increase the rate of reaction okay so here also you need the same enzyme so if i do the same reaction without the enzyme so around 200 molecules of carbonic acid will be formed per hour but if i do this in the presence of enzyme around six lac molecules will be formed in a second or per second see how much difference it has created so technically we say that it is increasing the rate of reaction now what is the rate of reaction product per unit time that means now it is producing more product with respect to the time you can also call the rate of reaction as velocity if you know the direction of the reaction you know it is going into a certain direction so we can use this word velocity as well now let's see how does enzyme work how does it work so for example this is the enzyme and this is the active site of the enzyme a substrate come or it arrives let me give you an example of substrate sucrose an enzyme is so grace so when the substrate will arrive it will bind to the enzyme and they will form enzyme substrate complex and this type of a state will be called a transition state that means it will come for a shorter duration of time it will be highly unstable because then it will form or uh it will get converted into the next state that is enzyme product complex in this state the bonds can either be formed or they can be broken they can be broken for example sucrose have to get broken into glucose and fructose that is a product and now enzyme product complex will form and later on the product will be released and enzyme will be reused again this is our enzyme function right this is how from outside it looks how it binds to the substrate and then convert it into but now technically what is enzyme doing there is one energy known as activation energy activation energy is energy that you need to start a chemical reaction so what is activation energy energy that we need to start a chemical reaction it's the energy that we need to start a chemical reaction so without this energy the compounds they are they cannot come together for example if i say you want to react co2 and water and they are at a high energy state they are moving here and there what if enzyme comes and bring them close together so that means it is uh making things easier for both the substrate how because now both the molecule will need less energy to make the bonds and that energy is activation energy so you can see here this is substrate this is product this is progress of reaction and here is energy you can see substrate is at higher energy level product is at lower energy level so when you are doing this the same reaction in the absence of enzyme you can see this much energy is required okay for example this is zero this is uh imagine this is 400 so around 400 kilocalorie of energy is required just vague i'm giving you vague figures okay now if i do the same reaction in the presence of enzyme maybe only 150 kilocalorie of energy is required okay so basically what enzyme is doing is enzyme lowers the activation energy barrier enzyme lowers the activation energy barrier activation energy barrier okay now what is the transition state a state where the bonds are broken down second thing here you can see the substrate is at higher energy level product at lower from here you got to know when substrate is converting into product the energy is released that's why the product is at low energy level so whenever the product is at low energy level this kind of reaction are exothermic because the energy has been released if product is at high energy level imagine the opposite would have taken place for example this is substrate product would have been here at higher energy then the reaction would be endothermic why because substrate was at lower energy when it got converted into product it took it took a lot of energy and it gets at higher energy level okay so that's how the enzymes were guys now what are the factors that affect the enzyme activity first is temperature second is ph third is substrate concentration fourth are inhibitors first is temperature how temperature affect the enzyme activity imagine the temperature is higher if you increase the temperature then the denaturation can take place what is denaturation breakdown of proteins enzyme will no longer can function but when you reduce the temperature the enzyme gets inactive let me give you an example why do we keep things in refrigerator so that there will be lower temperature and at that temperature no bacteria can function properly because their enzymes will be inactive and food will not go stale right now so if you can see in this graph this is this is uh this axis we have enzyme activity at this we have temperature you can see there here the enzyme activity is higher now at which temperature the enzyme activity is higher for an example for an instance take it zero take it seven and this one is around say two okay so at two ph uh okay so that's the temperature i'm really sorry take it around 0 take here as a 97 and take here as 36 okay so you can see at 36 degree temperature or the enzyme activity is higher okay so from here you got to know that this 36 degree celsius is the optimum temperature this is the optimum temperature because here your enzyme activity is higher same you can do it for the ph like in ph here also we have enzyme activity imagine this is a two ph and these enzymes are the gastric enzyme we say that gastric enzymes function at low ph so for them this will be the optimum ph so optimum at optimum ph the enzyme work uh in a better manner just like optimum temperature third factor is substrate concentration how does substrate concentration affects the enzyme activity let's take an example for example this is enzyme one two three four five six you have six enzyme and you started increasing the substrate concentration i added substrate so for example here the substrate adds or it will bind to the enzyme my graph will go something like this i added more substrate my graph will go something like this i added more substrate my graph will move further and here you can see out of six three molecules of enzyme have been attached with the substrate that means then they will form the product so i will say half of my reaction has been done here which is v max by two now i added more substrate more reaction more substrate more reaction more substrate more reaction and then the graph will go stationary why graph is going stationary the reason is because my sub enzyme is completely saturated my enzyme is completely saturated with the substrate so the reaction will go straight after vmax have been achieved the graph will go stationary why because here enzyme is saturated here enzymes are completely saturated okay so from here what you got to know on increase in on increase in substrate concentration the rate of reaction increases the rate of reaction increases this is what we have seen so far now the substrate concentration where v max by 2 have been achieved this one you call it as km km means michael is constant what is michael is constant guys this is michael is constant michael is constant says that it is that substrate concentration for example here it is like 30 millimolar just example so 30 millimolar is the km or michael is constant because it says at 30 millimolar the half reaction has been done or if i say three molecule of substrate here in in terms of this example so at three molecule of substrate concentration half reaction was done so michael is constant is that substrate concentration where v max by 2 is achieved or half of the reaction is done all right so this is how the substrate concentration can also affect the enzyme activity next next is inhibitor what are inhibitors these are something or these are substances that reduces v max that reduces v max or rate of reaction so they are doing opposite substrate concentration if you increase it they will increase rate of reaction if you will increase them they will decrease the rate of reaction so uh the function what inhibitors does you call it as inhibition what is inhibition the function which is performed by inhibitors that means inhibiting enzyme activity inhibition is of two type one is competitive another is non-competitive let's see what does it mean in competitive inhibition in competitive inhibition the fight is going on between inhibitor and substrate for example if i say this is the enzyme this is the active site okay here this is how the substrate looks like and this is how the inhibitor looks like this is inhibitor this is substrate now because both have these uh similar kind of shapes both can you know attach to the active site of the enzyme inhibitor have more affinity so it can easily attached and substrate will not be able to attach so if substrate is not able to attach product will not be formed and rate of reaction is not achieved this is what we say but what if what if i increase the army of substrate now substrate will will push back substrate will push back the enzyme and substrate will now bind to the active site of enzyme okay so on increasing the concentration of substrate i can pull away the inhibitor from active site and my rate of reaction can be resumed so what happen when you draw a graph of competitive inhibition this is what we draw in a normal graph like this here we have v max here we have v max by 2 this is the graph formed when you are not doing or you are not using any inhibitor this is km okay but when when competitive inhibitor comes at that time you need to increase the substrate concentration so that the rate of reaction can be increased now the graph will be something like that you will reach v max but when will you reach when you will increase substrate concentration earlier at three molecules the half of the reaction was done like here okay like here on three molecule half of the reaction was done but now i need to increase the concentration of substrate now imagine at six molecule half of the reaction is going to be done so here in a way my km of the this reaction will increase because what is km that substrate concentration where half of the reaction is done but now because i have to increase the army of substrate so that inhibitor should go away so here both enzyme both inhibitor and substrate they are fighting for active site so to pull away or push away the inhibitor i need to increase the substrate concentration to reach the v max of the reaction so when i'm doing so my substrate concentration is increasing and my km will also increase so here the substrate and inhibitor fights for active site okay and second thing in this reaction km will increase whereas the v max will remain constant v max will remain constant let me give you an example so we have an enzyme succinic dehydrogenase we have an enzyme succinic rehydrogenase its normal substrate is succinic acid its normal substrate is succinic acid right and its inhibitor is melonate so if some melanate will come here succinic acids concentration will be increased or we will if increase will we'll increase it and that can uh you know push away or pull away the malonate all right another examples of competitive inhibition in competitive we have some more examples so one we have done another example is methanol poisoning in methanol poisoning what happened generally people drink ethanol which is alcohol but if anyone accidentally drinks the methanol then you can add ethanol to the person's body so that methanol should not bind to the enzyme so what happened when someone drinks methanol methanol will be all right my pen drops so methanol will be converted into some poisonous material by the enzyme alcohol dehydrogenase all right that's why it's not ethanol poisoning it's methanol poisonous this is the enzyme in liver which will convert methanol which is the alcohol into an aldehyde and that aldehyde of methanol is very poisonous so what we do in that case we added like we added the uh like we have imagine one acting as inhibitor other acting as substrate okay so we are treating methanol as an inhibitor and now we will increase the substrate concentration that is ethanol and now ethanol will push away the methanol and it will bind to alcohol and methanol will then be removed from the body right this is what is the example of competitive inhibition so second third example is the bacterial pathogen in bacterial pathogen we use sulfur drugs sulfur drugs so sulphur drugs are you also used as a substrate which can be helped to or which can be used to kill the pathogens how imagine this is bacteria bacteria bacteria need bacteria need folic acid what does it need folic acid for its living it cannot take it from the outside environment it uses a substrate and enzyme to convert it or to form it it will use a substrate baba and enzyme e to form its product folic acid if you will somehow inhibit the enzyme so that no folic acid should be produced the bacteria can die so what we give them we give them this inhibitor which is sulphur drugs okay so you are increasing the concentration of sulphur drugs so that pava will not be able to bind and this is of folic acid can be cannot be formed and bacteria will die okay this is how competitive inhibition is about non-competitive so here the substrate and inhibitor were fighting for the active site here it is not fighting for active site here the inhibitor binds to allosteric site inhibitor binds to allosteric site this is active site to which substrate bind inhibitor this binds to allosteric site now what or how this graph will be formed imagine this is how you have formed the graph when there was no inhibitor this is v max this is v max by 2 and this is km this is km okay now listen to me very carefully here is this inhibitor has bind to the enzyme and now substrate will bind here substrate will bind here okay and this complex will be formed which is esi complex enzyme substrate complex and this enzyme will know will not term it will not leave the enzyme at any cost inhibitor will not leave the enzyme at any cost as a result this active sites shape will be changed and it will not be able to convert substrate into product as a result how much concentration you increase how much concentration you increase you will never achieve v max you will never achieve v max and as a result the km will always be constant km has nothing to do here and v max of the reaction v max of the reaction will drop or decrease so this is a very common question that is asked what happened during competitive and non-competitive during competitive co km increases v max remain constant here km will always remain constant a lot of you get confused in this why mam keyhem is constant because for this particular reaction km will always remain the same why because it has nothing to do with the substrate concentration the only thing here that matters is inhibitor has to leave the allosteric site even if you are increasing the substrate concentration active site is not capable to take it okay so here the example is cyanide poisoning so cyanide is a poison that uh you know inhibit the mitochondrial enzymes that inhibits the mitochondrial enzymes so that's about the inhibition guys let's talk about classification and nomenclature of enzyme first of all we'll talk about the classification we have divided the enzyme into classes which are further divided into 4 to 13 subclasses you have to learn all the classes in this sequence first is oxidative ductases second transferases third hydrolysis fourth lysis fifth and sixth are on next page okay so how many total classes six how many subclasses 4 to 13 first class is oxidoreductases so we have kept all the enzymes and the oxidoreductases which can undergo or which can catalyze the reaction of oxidation and reduction so if they are doing certain thing where something is reduced and other is getting oxidized that will be the oxidizes or dehydrogenases so enzyme which catalyze oxidation between two substrate s and s dash that is or they belong to oxido reductases transferases their name suggests they are going to transfer something earlier this group g group was with s and now it reacted with s dash and after reaction what we see the group went with s dash earlier s dash was alone now it went with status just like a friend came with a girlfriend and the friend asked this girlfriend or uh he they are going somewhere and this s dash is the friend of that boyfriend okay this is boyfriend this is boyfriend's best friend and this is the girlfriend now after some time the best friend took her girlfriend so what it is uh what is happening transferring of the girlfriend from one friend to the another right so that's what and this is how there is a the transfer is this work okay so transferase is the enzyme catalyzing the transfer of group g other than the hydrogen if it if it is doing the hydrogen's change or transfer that will be the category of oxidative reductases between a pair of substrate s and s dash hydrolysis hydro means water now on addition of water they will be breaking bonds right they will be breaking bonds like guys sucrase so craze okay so craze was breaking a bond which the glycosidic bond in the sucrose molecule but it needs water for that enzyme catalyzing hydrolysis of ester ether peptide glycosidic cc halide and pn bonds and all these bonds can be broken by that now lysis lysis are also breaking bonds then how they're different from hydrolysis they do not need water they do not need water if they are not needing water then when the reaction will be completed some molecules will contain double bonds okay so here enzyme that catalyzed removal of groups from substrate by mechanism other than hydrolysis leaving double bonds fifth and sixth fifth is isomerases includes all enzyme catalyzing interconversion of optical geometric or positional isomer they will convert one isomer into another like i have told you glucose and fructose both are c6h12o6 but both have different sugars they are isomers one is eldos another is ketos they both can be converted by this enzyme isomerases ligase is sixth g means glue enzyme catalyzing the linking together of two compounds it helps in joining two compounds just like we have dna ligase so they will be forming bonds like c o c s e and p o bonds can be formed okay now so how do you name them how do you do their nomenclature so nomenclature is in the form of digits like one two three four so this tells about one particular enzyme the first digit tells about its class second tells about its subclass third tells about is sub subclass and fourth tells about its individual enzyme for example for example i give you a code you're living in a city first of all first for example is a code for your city second is a court for your school third is a court for your class and fourth is a code for the role number in your class then they will get to know which student you are okay so we have done the classification only up to class for example i give you one example of five three two one tell me to which class does this belong fifth is a class isomerases so this belongs to fifth class okay this is how you can solve their questions all right now guys let's talk about the last topic and the most important topic with respect to neet point of view cofactors whenever i'm talking about an enzyme a complete enzyme which have everything and ready for catalysis is hollow enzyme hollow means complete so complete enzyme is known as follow enzyme and it is made up of two component what is uh one is apo enzyme p apo contains p so that's the protein part of the enzyme plus cofactors and cofactors are the non-protein part you heard it too true that there are certain non-protein parts of your enzyme they are sometimes always conjugated to them sometimes they are not so they make them the complete enzyme without cofactors the enzyme is incomplete it will not be able to do any work these cofactors are of three types prosthetic groups co-enzymes and metal lines these protective prosthetic groups these are usually attached to the protein part very tightly right so they are tightly bonded they are tightly bonded to the a point sign let me give you an example like heme heme is a cofactor for the enzyme like peroxidase and catalase right then we have coenzyme these are very loosely bonded and sometimes they are not even bonded they will only form bonds with the apoenzyme whenever it's needed so their union or bonding is very transient only during when they need to catalyze the reaction like vitamin b vitamin b act as a coenzyme for various enzyme because it contains nad and nadp so vitamin b is these two components nad and nadp which are basically nucleotides then like this is uh this is the nucleotide of adenine right so they are the one which bonds with the enzyme metal lines so metal lines they're also tightly bonded why because they also form coordinate bonds which bonds coordination bonds with the a point sign example zinc zinc is a cofactor for carboxy peptidase so without cofactor your enzyme is incomplete and it cannot cause the catalysis all right so from here the enzyme section is done in fact the chapter is done but let's solve some questions which of the following factors affect the v max of reaction inhibitor ph temperature all of these you know all of these answer four next enzyme catalyzing interconversion of optical geometric and positional isomer they belong to isomerase hydrolase ligase oxidoreductases very simple question from this topic one isomerases zinc is a cofactor four again simple carboxy peptidase now you must be thinking why it is like so simple question because you have just read the topic now next next is thank you so that's it and here we have completed the entire 11th class syllabus so this was a kind of a revision for you guys and uh maybe it's not just a revision in fact i taught you everything in much detail and i hope you will put some effort on that and uh you know have a great great scores in your school or whatever exam you're giving and uh we'll bring some more things uh just uh uh wait for some time we'll bring some more things interesting things for you you you just stay you know tuned with us and uh that's all we want if you want more uh more stuffs and more knowledgeable things in our channel here uh we'll definitely be working towards that because we have completed one series now and uh yeah i will be working for you guys will be working very hard for you so that uh you'll get to understand the each and every topic so i always believe that it's not just about uh completing a chapter or so it's about how how i can explain you things and how much knowledge can you get out of that right and that's the only thing and that's what education serves for you and uh that's the purpose of education and that's all and i really like a lot of students love me so much and from this i think a lot of you have also joined the keen english batch as well so i'll meet you there till then bye bye take care and lots of love and study hard keep working hard keep working harder until or unless you achieve your goal you know the hard work is the only thing that you can give it to yourself that's a promise from yourself to you only right so just believe in yourself and keep working hard nobody can take the thing that is yours so from here i just finish this up and bye bye take care thank you so much