hey chapter 3 biological macro molecules this is a bit of a long one I definitely usually break this um one lecture up into my two class periods that I do this week um usually it's like two 50 minute lectures within a little half hour activity after so I'm going to try to keep this to an hour and a half um but it might be really hard but I will try my best um side note if you've ever had nutrition or maybe you've just learned about this in your youth if you look at the side of a box and you look at the nutrition label uh there are certain things that give you calories calories are a unit of energy we think of them often as bad things but we need calories right every day because that's where we're getting our energy um to do our s reactions and where those calories come from are biological macromolecules um carbohydrates which you'll see carbohydrates and sugars sugars are really a small type of carbohydrate so carbohydrates proteins and lipids down here are your fats that's where your calories come from in your food you do have nucleic acids in your food um but they're small amounts and you don't really get much calories from them um you get a little bit of energy from them but they're typically used for something else which we'll get to at the end of this lecture just a little refresher on functional groups uh chapter two talked about functional groups these are um those chemical groups specific elements bonded in specific ways that give uh specific chemical properties and so our macromolecules are carbon it's like carbon bonded to other carbon uh hydrogen and oxygen those make up our macro molecules and then they have they'll have these specific functional groups on them that give them that property that kind of puts them in this broad macromolecule group the four main groups um so take a little time if you haven't to become familiar with some of these the amino groups really important we see those in proteins amino acids uh the phosphate group is important we see that in DNA in a phosphate group or I should say nucleic acids DNA and RNA we will also see it in lipids and phospholipids which will become more important um those are two big ones the carbonal group shows up as well a hydroxy groups you'll see a lot on things that makes things in alcohol and gives it polarity at least on that end and those are sometimes attached to the various functional groups but really the amino and phosphate are two I want you to um note and um hydroxy Carbono and carox are also important I'm going to go over each of these individually throughout the slideshow but uh we have four large classes of biological macromolecules so of course a molecule is made by a calent bond these are macro molecules so they're very large molecules they're one large molecule um made through calent bonding and other bonds will show up we'll see in a minute um that are used and needed by living things so we have carbohydrates lipids proteins and nucleic acids they are organic molecules and that is not in the way you're thinking of in um food being organic that is a different term uh organic molecules are means carbon base specifically carbon bonded to hydrogen so like carbon dioxide is carbon bonded to two oxygens that is not organ oric while methane carbon bonded to four hydrogens is organic so all of our biomolecules um are carbon based and they all have carbon bonded to hydrogen and oxygen shows up um in all of them there's a fair amount of oxygen except lipids I will say there's not as much oxygen but it is always there so all of them have carbon hydrogen and oxygen and then in some of the macro molecules you see some other elements coming in nitrogen and phosphorus or the two main ones that show up we'll see and then sometimes you have other elements in minor amounts like sulfur is one that shows up in proteins so macro molecules are very large molecules made up of smaller molecules the smaller molecules that they're made up of are called monomers they're very similar in structure and shape and they're bonded together in calent bonds to make what we call a polymer so if you think monomer 1 that's the single unit and then the polymer poly meaning many makes up the larger Macro Molecule made up of many of these smaller units bonded together um still being one large molecule um so all of our macro molecules are made into these larger molecules from solar molecules through a a reaction called dehydration synthesis um so this is generic to all of them I'm modeling it here showing saccharides which are carbohydrates so this is an example of sugars saccharides are simple carbohydrates um which you think of as simple sugars and so you have two smaller parts um two glucose molecules so each of these hexagon shown here are six carbon molecules they have every little corner which to doesn't show actually has a carbon and then there's another carbon here and this corner has an oxygen which is why the O is there um so you have this monomer of glucose that is going to be bonded to another monomer of glucose so glucose is our monomer here and this goes through a chemical reaction and enzyme would do this this doesn't happen on its own but enzymes in living things uh we'll put these together to make moltos so now this is went from two individual units to one unit this whole thing now is one larger oh let me take out the water the water on in it one larger molecule where they're bonded together in a CO valent Bond all right so let's look at some more things about this this is called a dehydration reaction because we are removing water from these molecules if you notice in red here we have an O group and a hydrogen and H those are removed to make the Cove valent bond that oxygen is there making the bond and water is removed so our product we actually make water it's going to release water when it does this but the water from the H2O and H and an O group are removed from each one from each of the monomer one o group and one hydrogen from each of the monomers to then make the larger Macro Molecule of Mose in this case and releases water so water is released in a dehydration synthesis which seems a little bit backwards because we're removing what would be a water molecule from our monomers um we make a calent bond and you have a polymer so in dehydration synthesis we are going from smaller units to larger ones we're going smaller to larger we're building up taking the smaller parts and we will be building larger Parts which will be building our polymers and these there can be many glucose added to have a long stet in them it'll be slightly different it won't be a dissect when you have multiple but you would still do a variety of dehydration synthesis reactions to make your large polymer so this is how we're going to make all of our macro molecules um the specific type of Co valent bond to make them has different names within them different macro molecules so we'll talk about some of those the opposite of a dehydration reaction is hydrolysis so hydrolysis is breaking down it's when you have a polymer some sort of Macro Molecule that is larger and you're going to break it down into monomers or smaller units sometimes there still might be like if this was a trisaccharide you might break it into a monomer and a disaccharide which needs to be broken down again but in this case we started with our disaccharide as our polymer and we're breaking it down to the monomer that make up the two monosaccharides so in this case we're doing the opposite uh it's pretty much the opposite of dehydration reaction so here we have to add water to our reactants so that we have an h and an O shown over here to be added back in when that Cove valent bond is broken so when that coent an enzyme would do this and living organisms would break it use water break that water and put an O on one and an H on an on the other monomer to have your two monomers so this is a hydris so when you hear dehydration reaction which can also be called a condensation reaction that is building up bigger making bigger macro molecules hydrolysis is breaking down um and adding water as we break that down to replace the O and H now will go through our four classes of macromolecules starting with carbohydrates so you've probably heard of carbohydrates you see it on the side of your food labels um it is a good energy source carbohydrates provide energy glucose being the main one that is a a monosaccharide a single sugar type of carbohydrate but all living things use glucose for energy it can also provide structural support So in general carbohydrates are used for energy and structural support or some types of energy storage they're very common in grains fruits and vegetables because plants make them if you've heard of plants doing photosynthesis which we will talk about later this semester um and you might have heard they make their own food that is because they are essentially making glucose using energy from light and carbon dioxide and water to make their glucose their sugars and then they form that they'll put it with other sugars or chains of glucose to store it which then we like to eat in our foods such as grains fruits and vegetables and depending on how it's stored is more of a um High sucrose with a lot of sugar might be in the fruits um some of the grains have more of the longer chains um to get to that glucose there's a generic formula for carbohydrates carbon two hydrogens oxygen and then however many there are so I'll talk about what this means in just a minute um I just want you to note here that carbohydrates generally are made of just carbon hydrogen oxygen that is pretty much all you find um there's a few exceptions but for the most part are carbohydrates are just that carbon hydrogen nitrogen and they're in this ratio of 1: 2: 1 so what does that mean so like glucose its chemical formula is C6 meanings it has six carbons h12 12 06 so I'm sorry for the background noise again they're working on the fifth floor I hope it's not too loud in there um there are the same amount of carbon and oxygens that's that 1: one ratio and that's shown here and then twice as many hydrogens right 1 to 2 to 1 so there's 12 hydrogens while there's six carbons and oxygen um three main subtypes of carbohydrates that I will talking about here monosaccharides disaccharides and polysaccharides monosaccharides are the single unit and this is the monomer of uh carbohydrates monomorph disaccharides disaccharides are so right mono means one d means two so disaccharides are two of those monosaccharides joined together um polysaccharides poly meaning many that's when you have lots of your monosaccharides bonded together can be a long chain or Branch change chains as is shown here monosaccharides are what you have heard of as your simple sugars um disaccharides can be simple sugars as well they typically have 3 to seven carbons they're often in a ring form shown here on the left um things that end in o are typically a monosaccharide or some of our disaccharides also in it o so when you see things they went in OS they're typically a sugar a mono or a disaccharide they contain a carbonal group and they're usually polar which is why they're sticky um so monosaccharides and disaccharides tend to be polar um which makes them kind of stick together and sticks to other stuff um what we think of sugar sticky when it spills on the floor and your kid doesn't clean it up um there are different um isomers of like glucose your book may talk about them a little bit more I don't really get into them but there's an alpha glucose and a beta glucose um depending if you look here which way the H and O are bonded but I don't need you to know that your book kind of goes into it more I do want you to note with with this ring structure you see these quite often you don't see a letter here it's assumed there's a carbon there I think I've talked I don't know if I've talked about this before but there's there's a carbon essentially there's always a carbon um every corner unless if it says otherwise like here there's not a carbon because there's an oxygen there but there is then a carbon there so um glucose is a six uh carbon molecule uh which 12 hydrogens and six oxygens uh and carbon makes four bonds so we can assume the carbon here is making one two um to the one to the H one to the O another one three to this carbon here and four to this carbon here and that's the five bonds that carbon is making um so monosaccharides they're a great energy source because particularly glucose because all living things have enzymes that can um readily take glucose and and break it down essentially to get energy out of it disaccharides are also um sugars that are made from doing two monosaccharides together and sometimes they can be the same monosaccharide or they can be different so sucrose this is your um sugar you use for baking table sugar baking sugar um the kind that a lot of people have in their Pantry easily to get the store um plants use this to essentially transport their glucose around so it's very common um it is sucrose is made up of monomer of glucose and fructose and through a dehydration synthesis reaction or I should say dehydration reaction your book for some reason has some weird stuff the way they word things um dehydration reaction moving removing the H and O glucose and fructose a five carbon sugar um are bonded together um and this is something I want you to note here in our saccharides our disaccharides and this is also in our polysaccharides when carbohydrates are bonded together their specific calent bond is called a glycosidic bond so you'll see glycosidic linkage maybe in your book or a glycosidic bond that's the specific type of calent bond that's going to bond our um monosaccharides together to make disaccharides and polysaccharides and it's not shown down here but water would be released as well because it's removing that water and we have enzymes of course that can break down sucrose into glucose and fructose and then we can use that glucose um there are different types of glycosidic bonds uh and your book goes into detail of them I will not ask you the different types of glyco bond I just want you to know that that's a type of coent bond that holds our um saccharides together Dy in polysaccharides together polysaccharides now are long chains of monosaccharides joined by glycosidic linkages so the glycosidic bonds here they can vary they might be different in the different types of polysaccharides um but it's still that type of bond it's a type of calent bond it's just there's some specific ways they held together that can be slightly different um polysaccharides are these long chains of monarchos saccharides so they can be branched or unbranched so they could be just like one long almost like thread like structure fibrous structure as what we might say or gly gin shown here uh which is used in animals for shortterm energy storage is highly branched um and it can have different types of monosaccharides right it might be made of one monosaccharide over over again it might be made of isomer So like um alpha glucose and beta glucose bonded together or it could just be different types of monoy themselves glucose fructose glucose fructose glucose fructose could be different stuff um they can be used for long or short-term energy storage so plants actually use use um starch which is their polysaccharide um for their long-term energy storage animals don't animals use fats for our long term but we do use carbohydrates or polysaccharides for a short term namely glycogen they can also be structural support fiber you may have heard fiber in your food you can't actually digest fiber it's one of the reason why it's good for you because um kind of the weight goes through can help quote unquote clean out not that you need it cleaned out but um your digestive system but but fiber is actually very strong and so um most animals can't digest fiber without having a specific type of bacteria to help them um and while monosaccharides and disaccharides tend to be polar for the most part polysaccharides tend to be non-polar so if you think about like your potato it's not nearly as sticky that's that potato in there is full of starch which that potato plant had made for its long-term energy storage when it can't do photosynthesis um and so it's full full of uh starch which of course then we love I love potatoes um because it's full of starch there's a reason we've evolved to like these things as well when fruits cuz we um have evolved to want to eat that um and so right they tend to be not nearly as sticky so they're usually non-polar but they're not carbohydrates are not classified as non-polar because lipids are fat group that is pretty much how they're classified as non-polar and insoluble in water well these can um generally be non-polar they're not completely and and it's only the longer chains the shorter ones are polar so they're not all classified as that your book kind of goes into more detail on the different types of starch and polysaccharides um I won't ask you anything more than what I cover in these slides so polysaccharides are kind of determined what type by their glyco linkages cuz there's different kinds your book gets into them you don't need to know them for this um but they essentially can cause the polysaccharides to be branched or unbranched depending on how they're bonded together um what like which type of glycosidic linkage um to common types of starch so starch is that generic term that plants use for their long-term storage um we have amalo um which makes unbrand so as the picture kind of up here shows it's more like a becomes a chain um amop pectin is Branched so you have these different groupings off um and plants can use these for longterm energy storage um and we'll see in the next slide how they can also use it for structural support So cellulose is a long unbranched chain of um glucose monomer so it's uh made of Alpha and beta glucose monomers and um it ends up making a long linear fibrous structure so cellulose did I say I hope I didn't say glucose at the beginning I said cellulose is made of glucose monomers cellulose is really strong this is what plant um cell walls are made of which will become we'll talk about this them more later in the unit but plant cell walls are made of um cellulose they they have like tubes inside them that move things around that move water around well I should say allows water to move around it's actually dead cells but the cellulos is there that gives it a strong support so um eating plants and this is why eating grass is really hard actually on a lot of animals most animals can't just eat grass because there's so much cellulose in there and they can't break it down and so ruminants those um hoofed mammals that do eat grass they have specific type of um procaryotes ARA in their gut that can digest the cellulose and that they use to help they use to help break down cellulose to get the nutrients out of grass so Salos is a strong um support structural support for plants kiten our good friend kiten I hope you remember from um a rly poly lab arthop pars that hard exoskeleton they have whether they're aolly poly a crab shrimp an insect a spider a scorpion um that excess skeleton is made of kiten uh fungi like um mushrooms um they also o have cell walls that are made of kiten so it gives them some support as well so kiten can be a good support um Ken's a bit unique in a lot of the carbohydrates it's a carbohydrate polysaccharide but it does have a nitrogen in it which isn't usually common um and kiten is actually something that we use as surgical thread as well because it can be so strong so we have taken to using kiten ourself but it kind of shows up uh a lot across living things as a good strong structural support on to our next group of macro molecules lipids you'll think of these as fats and oils and waxes um they are non-polar hydrolin that are insoluble in water and that is pretty much their loose definition how they are grouped together by being non-polar and insoluble in water um they are lipids are hydrophobic meaning they're water fearing right they're non-polar hydrop iic so I don't feel I think I've said this before it's not so much that they don't like water but more that water doesn't like them and so hydrocarbons they tend to be a part of our lipids our fatty acids and they're these long chains of carbon with hydrogen attached to them so we say hydrocarbons right there is oxygen um but not uh a lot right we think of these long chains of hydrocarbon with some oxygen so again oxygen shows up in all of our macromolecules but in lipids um it's not necessarily as much of it as there is in the other ones lipids are pretty diverse and have um a lot of important functions so long-term energy storage is really important to animals animals use lipids for their long-term energy storage we can get a lot of energy out of lipids which we will come back to next unit in chapter 7 plants and animals can both use lipids for insulation um that last picture right the adorable otter um they and you think of animals with blubber that's a fat right a nice fat layer to keep them warm some hormones a number of hormones are lipids are made of lipids um not all hormones hormones are chemical signals that cause reactions inside living things that cause something to happen um and things like you've probably heard of estrogen and progesterone oh those are lipids um they're really important for cell membrane so all living things have some types of lipids even when you think of like stuff that you don't think of being fatty every cell every living thing has a cell membrane and the major component of cell membranes are what we call phospholipids are kind of shown over there on the right I'll talk more about later and we will get into them in chapter 5 um so fats on the bottom there bottom leftish fats oils waxes phospholipids and steroids are like major types of lipids that we come across and I'll talk about some of these these so fats and oils are primarily made up of of glycerol and fatty acids those are like the two parts so lipids are a bit unique in that they do not have a true monomer all of our macro molecules the other three have true monomers lipids don't because of the way they're made so most lipids um there'll be some variation you see but have is a glycerol attached to fatty acids and so sometimes you'll see fatty acids as the monomer but it's not a quite a true monomer so um the glycerol which is kind of shown here chemically and the fatty acid which is then shown here this is the glycerol down here right this is the glycerol and then our fatty acid chains are here so this Esther linkage is the type of this is through the dehydration reaction and the type of bond that then is made um to put the fatty acid on to the glycerol and they attach and so the fatty acids are often like considered the monomer but it's not a true monomer because it's the glycerol up top there within all three if this big box down here at the bottom were repeated over and over again it could be a true monomer or if um let me do this for a second if it was like this if like this group was individually attached and then they were attached together you would have it be a monomer but it's not you have these separate parts you have the glycerol the glycerol here and then the fatty acids so you don't have a true monomer um this shown here on the left is a triglyceride you probably have heard of triglycerides we worry about too many of those in our blood um because they can have some negative Health consequences and we'll talk more a little bit about fats and um their health consequences so here's a triglyceride but we have our glycerol and fatty acids and um so your fatty acids are your long hydrocarbon chains and your glycerol is where it they attach to so our fatty acid chains generally can be what we say are saturated or unsaturated what's the difference well let's look here at the top our saturated fatty acid every carbon in this chain is attached to as many hydrogens as it can be it's a chain so it's going to make four bonds the carbon essentially before and after it and then so each carbon um can pretty much attach to two hydrogens except the last one which could of course attach to three so it is saturated with the hydrogens unsaturated fatty acids have a double bond in them a carbon remember carbon can make four bonds it has this double bond to a to the next carbon which means it can't make um it can't do another hydrogen it can only make a bond with one hydrogen not two so it is not or unsaturated with hydrogens because there's a double bond this double bond actually causes um a lot of things it causes a kink or bend as you can see in the fatty acid and that actually makes a big difference let's look at that on the next slide so saturated fat acids I have unsaturated on the next slide actually but saturated they don't have that double bond they're saturated with their hydrogen this means they can essentially peack tightly together so I'm going to draw this out kind of the bottom you have saturate that are generally straight and so they can pack together and stack together which means they tend to be solid at room temperature these are the fats you think of often as animal an fats although I will note that both animal and plants make both saturated and unsaturated fatty acids but you have higher amounts typically in animals um these are the kind that we we want to limit in our diet because these ones can get stuck in Our arteries um block things up cause issues because they are solid at room temperature and they stack together they can essentially create blockages inside of us which is a problem on the other hand our unsaturated fatty acids have that double bond and it's not shown here as bent but when you have that double bond that's when you have a Bend or kink in that fatty acid well if you have that they don't actually um stack together very well these types when you have unsaturated fatty acids they tend to be liquid at room temp temperature they don't Stack Up um and they're not they don't have quite as much of the negative Health consequences um right so they're they don't get stuck as much in your arteries and um have as much issues they're also more associated with plants because plants do make a higher amount of unsaturated but again both plants and animals make both types um and then of of course how many double bonds they have depends on what they're called so if you have a mono unsaturated fat that means you just have one double bond when you have uh polyunsaturated that you have more than one double bond so those could have like multiple turns in that um fatty acid chain you've probably heard of trans fats and how unhealthy they can be and they are so um CIS and Trans in biology refers to essentially kind of like same side or opposite side and we'll see this it kind of will come up again when we talk about organel we have a goldi CIS side and trans side um so the CIS configuration hydrogens are on the same side and when you have the hydrogens on the same side where you have that double bond between the carbons they um still have that Kink Bend and are liquid at room temperature so they're not going to pack tightly together terrains actually aren't a natural form they are made through industrial processing where the hydrogens are on opposite side so that's where the trans comes in is opposite well when you move the hydrogens if this can forcibly be done essentially um there's a way we can make it when that when that happens you still have the double bond in that carbon but you end up not having the kinger bend and so you still get the essentially straight line fatty acid even though it's unsaturated it's an unsaturated trans fat but um it's straight which makes it solid at room temperature and when they first did this when this was first made by the chemist who made it um and the company they thought that this was going to be better because we kind of knew that unsaturated fats tend to be healthier than saturated fats so hey here we have a trans fat that is unsaturated it's got the double bond but it's going straight um so we can it's not bending so this will be a healthier version for us and of course uh I was practically raised with that I had a lot of trans fats when I was a young kid and um probably isn't going to be good for me pretty soon so now we have found out um a while ago this was a couple decades ago how unhealthy and really bad for you that trans fats are they they are not very good and so margarine that was like a substitute for butter that was very common when I was young was full of trans fats it was made from trans fats but not healthy not good for you something you would want to avoid there are types of fatty acids that have um like these longer bends and chains um no double bonds here that are actually essential that are needed to some extent by living things um so some living things make this right there are um fish are well known to make omega-3 fatty acids this is essential fatty acid to humans um not all animals of course because some make it so they don't have to get it from their diet but of course humans don't make omega-3 and omega-6 fatty acids and certain nuts and certain types of things that tend to be high in protein talk about protein later um sometimes have these um omega-3 fatty acids in them in large amounts that are considered heart healthy and actually help reduce triglycerides so that was the few slides ago the triglycerides that can block in your blood um can help reduce them and considered um a part of a healthy diet I'll just say a little bit about waxes um waxes are long fatty acid chains modified to contain alcohols they are actually a decent energy source so like when you burn a candle right you're not burning the wick you're burning that wax around it the wax is the energy source the the wick is just kind of holding the flame um and of course they're hydrophobic as other lipids are but they help prevent water from sticking you've probably seen this with the candle right if you dip a candle in water the water kind of rolls off it doesn't the wax doesn't um melt in regular temperature water or dissolve or anything um so a lot of plant leaves have waxes some bird feathers have waxes particularly like aquatic type Birds um it helps that water roll off the surface um and can with plants can help help them hold in water as well in the leaf a really important lipid and probably the most important one for this class we are going to come back to phospho lipids in ch a little bit in chapter 4 and um a lot in chapter 5 so that is this unit so make sure you get to know them um a phospholipid is interesting you have two fatty acid chains the lipid portion attach to a phosphate group so you have your um glycerol here remember our glycerol but here we have two fatty acid chains attached and then instead of having a third fatty acid chain we have um a phosphate group of chats and this phosphate will often have other groups your book talks about them um you don't need to know the other groups there's just there's different types of specific phospholipid lipids depending on kind of what group is attach to it there the important part I want you to know is that it has this hydrophilic head water loving so this part of the phospholipid likes water because the phosphate here has a charge and this R Group um typically might be either polar or have a charge so the you have a polar head where you have these differential charges or partial charges um and nonpolar hydrophobic tails that fatty acid tails that don't like water and with a phospholipid this will be important particularly when we get to chapter five you have one saturated and one unsaturated there's two types each type and this is why I say all living things do have saturated and unsaturated fatty acids CU all living things have phospholipids in their cell membrane um and this is the major component of the cell membrane which I'm going to show on the next slide but important to know they have these two parts hydrophilic polar head hydrophobic non-polar Tails so if you take a bunch of phospholipids and throw them in water they'll actually spontaneously form a by layer that looks like this the and they essentially if you could think about this 3D it will make a a whole ball like if you can think of a basketball or some small it'll come around and form um essentially a ball but it will make a by layer at least across the water um and it does this because the Hydra philic heads are fine interacting with water they are happy to interact with water because they're polar and so inside and outside they can interact with water but the hydrophobic Tails do not want to interact with water and so they can be protected by being on the inside and not have to interact with water this polar hydrophilic polar head hydrophobic non-polar tail is called it has those two parts a phospholipid is made of those two polar hydrophilic non-polar hydrophobic tails and of course one fatty acid is unsaturated and one is saturated and that will become important later um and this is really important we call this a phospholipid Bayer and this is like a main component of cell membranes that helps control what comes in and out of fs and all living things cells the last type of lipid going to talk about here are steroids um steroids look a little bit different from the other lipids and that they have closed ring structur so these are those down here um they have these closed range structures but they're non-polar um hydrophobic structures that are insoluble in water and they have different structure uh structures functions so cholesterol cholesterol shown here if you notice it has an o group so that is a polar region o gives it a charge um so they can have Parts but cholesterol um is is important we think about it is like always negative cuz too much cholesterol in our diet is bad for us but we do have some and use some and need it in um our bodies brains and cells um it's part of the cell membrane it does have to cell membrane we'll talk about what it does for that later it's a precursor to other hormones so steroids are often hormones um hor testosterone right precursors cholesterol to make testosterone and estral which um s you need to make estrogen uh precursor to help make vitamin D and bio salts the bio salts that you use um to help digestion these come from steroids steroids hormones I think I mentioned earlier about being chemical signals um like you think of a hormonal teen they're sending out all these hormones that are causing reactions but you're really sending hormones constantly throughout your day it's just certain specific ones become very active during puberty um to cause uh sexual characteristics and secondary sexual characteristics and certain sexual development um but we have lots of types of hormones U many of them are proteins which I'm going to talk about proteins next but some are are um lipids lipid hormones which are typically types of steroids probably the most diversed and maybe me the most important Macro Molecule all our macro molecules are really important and they're all going to come up again um throughout the semester but the ones we will talk about a lot of our proteins and and nucleic acids um proteins are kind of across the board important come up everywhere nucleic acids come back up in unit 3 um all of them will come up to some extent next unit unit 2 as well so they're the most abundant probably because they're the most diverse they they just do lots of things lots of things are made up of them they range and function regulatory functions a lot of hormones I mentioned hormones before a lot of hormones are proteins as well so proteins and lipids are the most common type of hormones structural functions they're very important um in structure and support you've um probably heard of protein fibers your hair has a lot of protein your um cell membrane along with phospholipids has a lot of protein that's another major component of it um protective functions uh transport moving stuff particularly in and our cell and even within the cell enzymes um I think when people think of proteins they usually think of like a steak and that's a kind of structural function with um muscles but really when I think of proteins I think of enzymes enzymes do everything inside of you and all living things to be able to keep doing to build up and keep going they're doing all your reactions and all your reactions are done by enzymes um well I should say are sped up by enzymes so that they can happen in hopefully a reasonable manner to keep you alive and so enzymes are really important and um toxins toxins can be made of proteins as well if you get a wrong type of protein can be toxic um proteins are made uh I shouldn't say are made protein the information to make proteins is in your DNA which we'll talk about next uh Macro Molecule is nucleic acids and so the information to make proteins is in your DNA and then another type of uh nucleic acid called RNA is what is used to really make the protein and then once the protein's made it is the stuff that is doing all the work inside you keeping really keeping you alive all right amino acids um the monomer to proteins are amino acid so for all of these you need to know the monomer but getting your head around amino acid being the monomer to protein is really important um you've probably heard of amino acids they're nutrients you need them some amino acids you can make some you cannot make so some we have to get from our diet um they have a general generic structure like our monomers um they have an amino group so remember our um functional groups there's AO group there's a central carbon there's always a central carbon that's important and there's a carox group and there's a hydrogen those are the same across all amino acids so proteins are made up of these linked together um and they all amino acids have this as the same part but where they vary and really what makes them different is what we call this variable side group or this R chain or side chain the we we call it a variable R Group this differs the elements it's it can be Rings sometimes it's carbon Rings it can be almost like a fatty acid it could be just a hydrogen what elements and the form they're taking varies on this our side chain um and that gives the amino acid its particular chemical properties there are 20 different amino acids like I said some you can make some of these you can make some of them you have to get from your diet and they do have groupings together so what is highlighted in blue is that variable R Group so with all of these um they kind of show it a little differently here don't they they um moved our carboxy group for some reason um but you have your amino group carboxy group and uh your hydrogen and then in blue are all these variable side change the this is that r that changes so like some of them I said can just be a hydrogen some of them might be a short chain some of them can be a long chain some of them can be these larger ring structures some of these R groups can be pretty dang large tryptophane is kind of huge there and they're grouped by if they're essentially kind of non-polar polar or have a charge so like nonpolar R groups um are in this group non-polar doesn't like water um so this will be important when I talk about protein folding the non-polar Parts like to be on the interior part of the protein where maybe it's not interacting with water the polar then you have polar um right they have a difference in charge oh so those might interact with water um you have uh charged these have a charge on them and if you notice those have a positive charge and then these have a negative charge so they can have um a different type of charge where if these are in different parts of amino acid the ones with a negative charge could be attracted to the ones with a positive charge and make a bond and that can help it fold which I'll talk more about later um and these are also non-polar but they're kind of grouped in how like these large ones these are kind of like two of two subsets of a larger non-polar group you have non-polar but then you have like the large ring what we call aromatic R groups where they make the ring structure or the more chain simpler structure and non-polar ones I'm glad they went back to I don't know why they on the last side but they're back to our Amino and our caroal the way I'm this is the way I'm used to seeing a uh Amino a it so they just have the H at the bottom oh they have so weird they have the r here but then they don't have it at top sometimes I don't understand Open Stacks images but let's pretend this is our R Group then um and the r can kind of sometimes shown at the bottom or top typically it it doesn't matter it's the same way but amino acids are linked the important part here that I'm trying to get to amino acids are linked by peptide bonds so this is a dehydration reaction um and we have the amino in is kind of always what we think of the start end and the carboxy end is the end where another one could be linked because you do you go from your carboxy end of one to the amino end of the other and in doing that when you're doing your dehydration reaction you're going to remove the O and the H and make water and you are going to make a CO valent bond between amino acids and that specific type type of calent bond is called a peptide bond remember that because it's going to come up I will probably ask you it on the test I know in unit 3 I may ask you it on this test but it always comes up in unit three again as well so peptide bond joins one amino acid to the next amino acid proteins the thing about proteins is they have specific level of structures and they have to be folded in a specific way for them to work right so they have four levels although not all sometimes many only go to the third level but I'm going to talk about each of these in separate slides there's a primary structure a secondary structure a tertiary structure all proteins a proteins is really typically not functional until it's at its tertiary structure some proteins need to be at a quinary structure to be functional and I'll talk about what each of those are on the following slides um but just know with all of these amino acids um are important in um um their order how they're put on they're all going to be put on and we'll see how this looks sorry I just got a little email pop up and it dinged I don't know if you heard that or not sorry if you did our first level structure is the primary structure you might also see this as like that first primary that's shown so if you see that it's a primary structure this is just the order of amino acids the amino acids are bonded together one amino acid this is representing there's 20 different amino acids they all have a name this three letters are representing the name of the amino acid I think that's I don't know if it's glycine or um there's two that start with gy but I forget the other one is glycine to isoline maybe but to valine it's one amino acid to the next amino acid and they're bonded together in a peptide bond it's not shown here but you would have your Amino end and your Amino would be here and your carboxin would be there um and they're bonded together um this is another primary structure um some we'll get to it in a minute but some proteins are made up of more than one amino acid chain and so this is like the two chains that are going to make up this protein at some point the sequence of amino acids is called a polypeptide or a polypeptide chain so a polypeptide chain is a sequence of amino acids the primary structure is the unique sequence of amino acid so the primary structure makes a polypeptide um know that the order your amino acids are in bonded together in peptide bond makes a polypeptide chain it's just think of it as a like beads on a string a long string of amino acids bonded together um with peptide bonds and that makes up a polypeptide and that's our primary level of structure in a protein primary structure primary structure is important cuz that order of amino acids is causing how the protein is going to fold and function which I will get more to in a few slides so having the correct amino acid in the correct order of that polypeptide chain is really important um CLE cell anemia is a genetic disorder that causes blood cells to sickle after they give up the oxygen um and then they don't carry as much oxygen so people with CLE cell anemia tend to be anemic low oxygen low energy and um can have a variety of health issues associated with that disorder um luckily there is a new like brand new genetic um essentially Gene editing treatment for this something called crisp um that's very expensive so it's not going to be able to help everybody um and there are treatments to help with quality of life but the new crisper is completely GameChanger for it because it can actually change the gene because with CLE cell anemia one um amino acid in the genome uh I believe it's just one base pair causes one amino acid to be changed on the polypeptide chain that is made at the primary structure and that one amino acid change from glutamic acid to veine is what they're showing here uh causes the hemoglobin protein in blood cells to behave differently structure becomes different and it functions differently um and causes this can which can be a pretty severe Disorder so primary structure is very important and hopefully as we go through the next levels you'll also see why um these order of amino acids makes a difference in how it folds primary structure is the amino acids being bonded through a peptide bond so being bonded coal to other amino acids in a specific order so coent bonding is responsible for that primary structure the secondary level of structure of proteins is caused by hydrogen bonding um essentially hydrogen bonding between the um Carbono and amino groups in the amino acids right all the amino acids have that there will be a hydrogen bonding between them and it makes um that string of amino acids kind of fold up more like um kind of accordion like it's not exactly but maybe a way of thinking of it and we call that a beta pleated sheet or um if it's still a hydrogen bond but a little bit different in the way it bonds um it will make an alpha what we call an alpha Helix which is a helical like spiral structure so um the secondary level of structure the pro the poly peptide I should say it's not a protein yet or functional protein I should say but it's on its way there um at the secondary level we start getting folding but the type of folding so like a three-dimensional shape we get is Alpha Helix which is shown here in this helical structure and shown here over here in the way it's bonded or what we call a beta pleaded sheet which is kind of that's sort of the way it looks and then how it looks chemically your book goes in a bit more detail on um how it the bonding the hydrogen bonding it's making you don't need to know all the details I just want you to know that it's a alpha Helix Orba petus sheet due to hydrogen bonding for the secondary level of structure primary structure peptide bonds which are calent bond order of amino acid makes the polypeptide chain secondary level of structure hydrogen bonding um between the carboxy and the amino groups that all amino acids have creates beta ple or Alpha Helix sheets tertiary level of structure is now where we can get a functional protein the protein is going to fold um up into a three-dimensional shape now to make its actual structure where it can function potentially most proteins I'll get to it in a minute um so this tertiary structure is due to chemical interactions between the r groups so this is why it's really important where the amino acids are on the Chain because that R Group that's on all those amino acids are going to bond like the remember how we looked back at the amino acids there were positive ones and negative ones those positive and negative ones can Bond and make ionic bonds um you can have our groups that have where is I going to look here disulfide linkage that's a type of um calent bonding so that's sulfur there um it's a very strong bond that holds it together so these would be amino acids where this R Group and this R Group on those amino acids on that part of the chain are making bonds to each other you can have hydrogen bonding so here we have a hydrogen bond between different R groups that are uh amino acids in different parts of the change hydrophobic interactions remember that um hydrophobic R groups don't like water um proteins are typically made in an aquous solution cuz they're even for terrestrial organisms they're inside of it which is in for the most part aquous solution so um a lot of times the hydrophobic R groups get pushed towards the interior of the protein um and those hydrophilic um our groups will be interacting with the outer part of the protein like interacting um in the cytoplasm or one cell membrane something where it could be okay with water so all these different interactions and bonding are occurring to cause the protein to fold up into a three-dimensional shape that now has function and most proteins are like this if a protein is made up of one polypeptide so it says here a structure of a polypeptide um at the tertiary level structure that's as far as it'll go this is the functional protein some proteins are made up of more than one polypeptide in those cases we have another level of structure where those polypeptides go through each of these up to the tertiary but then they come together to make the next level so for a majority of proteins this is the highest they go if they are made of one polypeptide chain um the tertiary structure is as high as it goes some larger proteins are made up of more than one polypeptide in this case we have a quinary structure which is like a fourth level structure where multiple polypeptides have now formed and they come together so hemoglobin this is a picture of hemoglobin here is a very large protein and it's made up of four polypeptide chains um quary are if there's two or more polypeptide chains so once you have two polypeptide change that come together to make a protein it's at the quary level if it's just one poly chain that folds to make a protein it's at the tertiary level so here you have for each of these colors represents a different polypeptide chain that each has their um primary structure and then their secondary structure Alpha Helix beta plated they're tertiary structure where they're folded up if you know notice they all look folded up and then they have bonding together to cause it to come together as this large um protein with of what we say is like subunits like polypeptide kind of has a subunit with hemoglobin you have like two beta chains so these polypeptides are essentially the same but there's two of them and then there's two alpha chains which are essentially the same and there's two of them and then all four of those come together and you have a large protein at the quary level so here's a nice little summary I kind of divided it because to be able to make the images a little bit bigger I separated out so it looks a little goofy sorry about that but our primary level primary protein structure um right is the amino acid sequence which is a polypeptide chain made of calent bonds amino acids calent bonded together through dehydration reaction um with um pep specifically peptide bonds uh polypeptide chain that primary level polypeptide chain will then um fold up at the secondary level to have some sort of more um structure to it and this one is due to hydrogen bonding and it will generally form a beta plated or Alpha Helix sheets and I should have noted there back there with um our polypeptide chain some proteins at their secondary level are all beta plated or all Alpha Helix um a lot have a mixture of both uh certain regions maybe they might have more Alpha Helix and just a few beta pleed but they can be all or both or one or the other um and then our tertiary level now we can have a functional protein that folds up in its threedimensional shape and um they're kind of showing you how like within this protein folding there is the sub folding of the alpha Helix and beta plated sheets and then due to all the interactions of those R groups so the r groups where the amino acid is and how it bonds to other amino acids um based on the R Group with hydrogen bonding ionic bonding calent bonding hydrophobic interactions um are going to cause it to fold up in a three-dimensional shape which it may function at this level or if it's made up of two or more polypeptide chains as shown by the two different colors of blue here uh or shades of blue I should say you have the quary level we have our levels of folding to make our functional protein so that's going to be shown over here on the left in this normal protein folded up well that folded up three-dimensional shape of a protein let's say it's at the quary level is due to that different bonding environment can change those bond that bonding um if the pH changes right that's the hydrogen ions in a solution hydrogen ions can interfere with bonding if the temperature changes heat has energy and can break bonds salinity are ions in a solution which can affect bonding all of these things if they pH temperature and salinity increase or decrease too much to what that protein has evolved to work in right it has a normal range that it can function in within a specific specific pH specific temperature specific solinity if it gets too far out of that range it denatures denatures is essentially coming apart um I have here changes in molecular bonding and structure your book had a more specific definition to protein I tried to keep this more generic in the notes because all of our other macros other macro molecules can denat too DNA we say denatures when the two strands can come apart and we can do that artificially so D nature isn't specific to proteins but we think about it with proteins mostly so um the protein can essentially fall apart and denat back to the primary level typically with denaturation um it's the primary level structure is going to fall apart because that is completely made of calent bonding which is very strong but at that um tertiary level you have ionic bonding going on and hydrogen bonding which um have strength but if you're going too far out of the pH temperature solinity those come apart and so it's going to come apart and um even if there are some calent bonds there they're probably um it's not completely made of calent bonding at the tertiary level structure so it kind of falls back to the primary level and we call that a denature prot prot so now it's a nonfunctional protein when it's denatured right because it is not working at the primary level some proteins can renature renaturation here where they can if conditions return go back to that normal protein like they will refold and go through those levels of structure so like a pH may cause the protein a higher low PH may cause a protein to denature and come apart to its primary structure but when the pH returns to the normal range it can potentially renature not every protein that gets denatured can renature there are certain things conditions that have to be it might depend how far right if you get way too hot nothing's going to come back together if you're disintegrating the whole thing um that would not work but uh right cooking an egg you are denaturing those proteins in the egg and that is an irreversible denaturation you can't go back to a liquid egg or you know have that liquid um whites after you have cooked an egg um but inside living organisms a lot of proteins can renature if things get a little out of whack but not too far that's the homeostasis might be trying to bring it back so it very much depends on the protein and the condition how high temperature salinity or pH is all right our last Macro Molecule I'm going to talk about are nucleic acids you've probably heard of DNA and maybe you've heard of RNA um but nucleic acids are the genetic material of living organisms so they essentially hold the information to make organisms or help um turn that information to make what's needed for the organism um we'll get more into how that works in unit 3 but we have two types of nucleic acids what we called deoxy ribonucleic acid which is DNA that's what DNA is short for deoxy ribonucleic acid it's a mouthful and then we have ribonucleic acid and that is RNA um deoxy ribonucleic acid is shown here on the left as the double stranded double helix classical shape um and the ribonucleic acid is single stranded um on the right and over here on the far right is of course uh representing DNA what do these things do in this cell um your book in this chapter goes a little more involved into or a little more in depth I should say into what RNA does I cut a lot of that out of the slides because we go over the whole process that they're kind of talking about there in unit 3 pretty deep so you're welcome to read about it it's a good idea to to have that will help when we get to unit 3 make a little more sense if you've kind of heard it or seen it before but I took it out of here because I feel like it's kind of complicated um and it's a little hard to skim over so um I'm going to go over some of that RNA stuff more later I just try to keep it as basic as I could for um the notes so DNA codes for The genome of the cell the genetic content essentially The genome has all the information to make you to make everything about you and for that living organism the DNA has all the information to make that living organisms um DNA codes for proteins but proteins are enzymes and structural uh transport so those proteins are made then to make the things you need to break down the things you need to build up the things you need to make your cells to help divide your cells um to process energy to maintain homeostasis to make the hormones to think something to happen to respond to stimuli all that stuff is essentially done by proteins which is the information for the proteins is in the DNA so DNA has that information um and all that information is in every cell because you have the all your DNA is in every cell you have but you don't need all that DNA turned on in every cell right in your eyeballs you don't turn on the cells um that you're needing or I should say turn on the genes that you're needing to grow toenails and you're not turning on the genes that make hydrochloric acid in your stomach you otherwise you'd be having hydrochloric acid in your eyeballs and that would really burn and hurt so you turn off sections of DNA in each of your cells um once they kind of get their specific rol certain things are turned on and off to depending on how it's used and sometimes things can go wrong with that which can cause a variety of issues um DNA also have the some information to help make some of the RNA so RNA is typically made from DNA which we'll get to later which sounds a little confusing um but DNA also makes the proteins that are then needed to make the RNA um DNA has the information but it doesn't actually do anything like there's this double stranded DNA and these little colors here are base pairs and those order of base pairs is the information for a gene but what it is is the information that information has to be read which is what we call transcription and then it has to be translated which we call translation to turn in to make it into a protein so DNA holds information and that is passed on um from parent to offspring and we'll get into how that is done next unit but it's what gets passed on it's the hereditary information but RNA is in making those proteins so is part of protein synthesis the DNA has information for the proteins but RNA is really the worker horse in translating that information to take it from DNA and make it into the protein so RNA is really important um in making the proteins needed to make you and living things DNA and RNA are quite similar um in their monomers so their monomers are nucleotides is what our monomers of our nucleic acids are hopefully that's not too hard I feel like nucleotides are the monomers of nucleic acids um so nucleic nucleotides I should say have three parts they have what we call a nitrogenous base which is shown here and so it's like these nitrogen ring structures with carbon and hydrogen um and these have slightly different um sizes and organizations we'll talk more about the nitrogenous base in a future slide um there are two types of nitro two generic types um perianes and purines and then there are certain types of perianes and purines of each of those which we'll get into in a minute then there is a pintos which just means five carbon sugar so go around here there is a five carbon sugar and this is different this sugar is different whether it's DNA or RNA so in DNA it has deoxy ribos so there is an H off that carbon off the second carbon so this is the first carbon second carbon third carbon fourth carbon fifth carbon that's going to be important in a minute um and in deoxy ribos there's a hydrogen off that second carbon in RNA ribos sugar there's an O group there and that's the only difference in the sugar it's just the sugar slightly different there's a o group so DNA is deoxy ribos um RNA is ribos sugar and then one or more phosphate group so in the DNA RNA um when the monomers are put together to make a polymer it's one phosphate group but the nucleotides themselves can be with one phosphate group there can be another phosphate group two phosphates and there can be another three phosphates and we'll we'll get into that later so they have different ways they show but in the polymer for form there's only one phosphat but in nucleotides there can be one two or three phosphates those nitrogen bases that attach to the sugar are either what we call purine or peridin um they're both found these nitrogenous base structures are found both attached to the ribos or deoxy ribos sugar uh for the most part there are some differences so the purine they both can attach to the sugar so um adenine can be what we call a base pair of DNA where that Adine is attached to deoxy ribos or it can be attached to ribos um and be a what we call base pair in um RNA and guanine as well and if you notice purines have what we call a double ring so see this the structure the nitrogenous base has two rings so they're similar in structure but they have some differences if you notice the chemical differences where these things are peridin are single rings so they have single rings and then it's a little bit different what we find in DNA and RNA so CIS um cyto that wrong cyto is found in both DNA and RNA so this nitrogenous base will bond to deoxy ribos or ribos thymine on the other hand is only found in DNA um so it only binds to the deoxy ribos and uril which is very similar very similar structure slightly different is only found in RNA so it only binds to our ribos sugar and purines and peridin can bind to each other through hydrogen bonding which I'm going to show you in a minute um and you may have heard of this before but we say a so Adine is represented by a Adine will bond to thyine so we say A bonds to T and guanine will bond to cytosine um so we say G bonds to C or c bonds to G uh through a hydrogen bonding and I'll show you how later um and then a can in RNA a can bond to uracil as well uracil and Adine can bond in a hydrogen well the nitrogenous bases can Bond regardless of it's in DNA or RNA which we'll see when we get to unit three let's look at the structure of DNA DNA is generally what we say double stranded although these two strands can come apart that actually can be called you can denature them and make them come apart or enzymes can separate them um RNA is typically single stranded so there's only one strand so it's double stranded um and they have a sugar phosphate back bone so we're going to zoom in here this over here on the left is kind of just showing the sugar phosphate backbone just has a line but let's look in chemically at this is what is the sugar phosphate backbone because here we have our nitrogenous base but the sugar and phosphates are What bond to each other along the backs side so you have phosphate and you notice there's a number five Prime here so where this says five Prime that is because that phosphate is attached to the five Prime Carbon on the sugar so this was our sugar and this was one second carbon third carbon fourth and then there was a fifth carbon that was attached that the phosphate group is attached to so that's the five Prime end and then if we go down this way we see a thre Prime um and this is a little here this is our five Prime and if I follow this down I'm going five Prime to three prime um this is like if that double helix was untwisted over here on the right where I'm drawing out if you notice this sugar here the dioxy ribos sugar here um this three prime carbon has this o group so this is where if I was going to add a new base pair I would have to add it to here to the three prime end because when we get to unit 3 you'll see that the enzyme always has to add a new base pair to the three Prime in it can't put a new base pair on this way when it's adding base pairs to DNA and if we look at our other side let's look at our other side it's going to be opposite they're kind of like these are almost like they're upside down we have our five Prime end here so this is our phosphate group five Prime carbon here and the three prime carbon is down here with that o group so what we say DNA runs is anti-parallel if it's five Prime to 3 Prime on one side the oppos the other strand is opposite five Prime on the other end to three prime so if you know one I have gave you this picture and I only put the five Prime here you would could tell or know what all the other sides are and its orientation um and then we have our nitrogenous space they stick out towards the middle our nucleotides stick out that way towards the middle and they make these what we call the rungs of the ladder they're making hydrogen bonds to hold the two strands together so there are two hydrogen bonds between adenine and thymine between their nitrogenous based ring structures they make two hydrogen bonds you notice those double do do dotted lines because dotted lines are hydrogen bonding and then cine and guanine make three hydrogen bonds between them and they stick out so c bonds to G and G bonds to C and T bonds to A and A bonds to T they make hydrogen bonds um so we have opposite we have what we call complimentary base pairing complimentary pairing where those base pairs always if you know one strand you know the other strand and it's orientation if you know the orientation of one so it's really nice because if you have one strand of DNA you can make another strand of d DNA from it so here's another picture of showing them running anti- parallel 5 Prime 2 3 Prime so that means this side is 5 Prime to 3 Prime of course it's untwisted here and because you know what bonds you can know what a DNA what one Str of DNA is you know the other because they're complimentary so if I say 5 Prime g c a g 3 Prime sorry for that being so messy you know the other side is 3 Prime G bonds with c c bonds with G A bonds with T and G bonds with C five Prime you know the other side would run that way this is called anti-parallel when one which I think I had on the previous slide but we have it here too when one is five Prime five Prime in to three Prime in and there's our phosphate group on that five Prime carbon and there's that three prime carbon open so that's a three Prime in um it's anti- parallel because the other side is 5 Prime to 3 Prime um the bonds between I should have mentioned this maybe I should have mentioned this before but I think that's why I wrote on the slide so I wouldn't forget sorry for the background noise if you're hearing that all that construction when a new nucleotide right nucleotides will be added one at a time this would be added next if this was our strand I know what this is I would know what goes here there are three base pairs so C and G um it's going to put the um what is this I think this is G and it's adding C if it's adding this see here this phosphate is going to bond to this this group here right the um from the three prime sugar and so this Bond made with that um new nucleotide is called a phosphodiester bond that's another type of coal Bond right and then when it puts the next nucleotide on here the enzyme that would do this we put this nucleotide makes another calent phosphodiester Bond so the nucleotide itself is held together in Cove valent bonds and one nucleotide to the next nucleotide that sugar phosphate backbone is held together in calent phosphodiester bonds but the two strands are held together by hydrogen bonding so the two strands can separate fairly easily because that's hydrogen bonding but you don't break apart the DNA backbone easily cuz that's coent bonding the other thing because you have these three hydrogen bonds between C and G and two between um a and t regions with uh High CG content regions of DNA that have a lot of C's and G's tend to be stronger and hold together a little bit stronger than regions with high a and t where you have a lot of a and TS they can break apart a little bit easier because you just have the two hydrogen bonds holding them together but they're all hydrogen bonds so they can be broken with specific enzymes or um heat as well so as I said before well let's do this one as well or think about it I'll start and then you can finish if you want to see if you know it if it's five Prime to 3 Prime with that DNA sequence the other strand would of course be three oh not showing up very well three prime t a g c and hopefully you would know the rest few things about RNA like I said your book goes more deeper into RNA so if this seems a little confusing and you want to read that for more background you can um I will only ask you on the test what I go over in the notes so RNA is used to make proteins um but there are different types of RNA so RNA is for the most part single stranded but RNA can fold up to be like a protein and um RI zones which are we will learn about those in chapter 4 um are little structures that where proteins are made and they're actually made of RNA folded up with um they're associated with some small proteins themselves and those are the little organel where you make proteins so ribosomal RNA is the RNA strands that are found and that are folded up and found in ribosomes so we call them ribosomal RNA or R RNA messenger RNA is a single strand of uh RNA that is made from the DNA so the information that has the gene the DNA strands will separate it would actually separate into two strands and then I'm going to show this in blue RNA will come on one side and essentially make a strand complimentary to the Strand it's using and that is going to be messenger RNA and that's getting the information from the gene from the DNA that has information from that Gene and takes it off to the ribosome to turn it into a protein so messenger RNA or mRNA is really important we'll go into all of these in unit three and then transfer RNA is the RNA that brings the amino acid to the ribosome so it has it's a long strand of RNA um that based on the messenger RNA will match up to bring the specific Amino Aid so that you can make your polypeptide chain in the correct sequence in that first primary order of structure so Transfer RNA is called TRNA it just carries amino acids to the ribosome there are other types of RNA but for the most part this is all we really go over in this class um and we will get more into these in unit three but RNA actually does a lot of stuff in the cell so there are different um some other different functions um but typically RNA most of it is used in some way of making proteins or regulating making those proteins and here's just a nice little summary of DNA and RNA um I hope that help you understand um the macro molecules