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Overview of Biological Molecules for A-Level

Apr 23, 2025

Miss Estrich's Biology: A-Level Topic 1 Overview - Biological Molecules

Introduction

  • Overview of Topic 1 in A-Level Biology: Biological Molecules
  • Key facts for quick revision
  • Detailed explanations available in additional videos and notes
  • Upcoming release of an active recall workbook

Monomers and Polymers

  • Definitions:
    • Monomers: Smaller units that form larger molecules
    • Polymers: Made from many monomers bonded together
  • Examples:
    • Monomers: Glucose, amino acids, nucleotides (RNA, DNA)
    • Polymers: Starch, cellulose, glycogen, proteins, DNA/RNA
  • Reactions:
    • Condensation Reaction: Joins molecules, forms chemical bonds, releases water
    • Hydrolysis Reaction: Breaks chemical bonds, requires water

Carbohydrates

  • Types and Examples:
    • Monosaccharides: Glucose, fructose, galactose
    • Disaccharides: Sucrose, maltose, lactose
    • Polysaccharides: Starch, cellulose, glycogen
  • Glucose Structure:
    • Alpha and beta glucose are isomers
    • Formula: C6H12O6
    • Differences in hydrogen and hydroxyl group positions
  • Disaccharides Formation: Glycosidic bonds through condensation
  • Polysaccharides:
    • Starch and Cellulose: Found in plants, function as energy store and structural support
    • Glycogen: Found in animals, energy store
    • Structure-Function Links: Amylose (compact helix) and amylopectin (branched), cellulose (fibril structure)

Lipids

  • Types:
    • Triglycerides: Glycerol and 3 fatty acids
    • Phospholipids: Glycerol, 2 fatty acids, and a phosphate group
  • Properties:
    • Energy store, insoluble, hydrophobic
  • Fatty Acids:
    • Saturated: No double bonds
    • Unsaturated: At least one double bond
  • Phospholipid Properties:
    • Hydrophilic heads, hydrophobic tails
    • Forms bilayers in water

Proteins

  • Structure:
    • Amino acids as monomers
    • Formed through condensation reactions, peptide bonds
  • Levels of Structure:
    • Primary: Sequence of amino acids
    • Secondary: Alpha helix or beta pleated sheet, held by hydrogen bonds
    • Tertiary: 3D shape, held by ionic, hydrogen, and disulfide bonds
    • Quaternary: Multiple polypeptide chains

Enzymes

  • Function: Catalyze reactions by lowering activation energy
  • Specificity: Unique active site complementary to substrate
  • Models:
    • Induced Fit Model: Active site molds around substrate
  • Factors Affecting Activity:
    • Temperature, pH, substrate concentration, enzyme concentration, inhibitors

Biochemical Tests

  • Starch: Iodine test
  • Reducing Sugars: Benedict's test
  • Non-Reducing Sugars: Acid hydrolysis followed by Benedict's
  • Proteins: Biuret test
  • Lipids: Ethanol emulsion test

Nucleic Acids: DNA and RNA

  • DNA:
    • Stores genetic information
    • Structure: Double helix with complementary base pairing
  • RNA:
    • Ribose sugar, uracil instead of thymine
    • Functions in protein synthesis

DNA Replication

  • Process:
    • Semi-conservative
    • DNA helicase and DNA polymerase involved
  • Historical Context: Watson, Crick, Franklin, Meselson, and Stahl

ATP

  • Structure: Nucleotide derivative, energy carrier
  • Function: Provides energy for cellular processes

Water

  • Properties:
    • Metabolite, solvent, high heat capacity, large latent heat of vaporization, strong cohesion

Inorganic Ions

  • Functions:
    • Hydrogen: pH balance, respiration
    • Iron: Hemoglobin
    • Sodium: Co-transport
    • Phosphate: DNA, RNA, ATP

This overview provides essential knowledge areas in the study of biological molecules for A-Level Biology, highlighting structures, functions, and biochemical significance.