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2. Biological Molecules

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  1. 2.1 Testing for Biological Molecules

    1. 2.1.1Benedict's test for reducing sugars

      • Benedict's test for reducing sugars

    2. 2.1.2Iodine test for starch

      • Iodine test for starch

    3. 2.1.3Emulsion test for lipids

      • Emulsion test for lipids

    4. 2.1.4Biuret test for proteins

      • Biuret test for proteins

    5. 2.1.5Semi-quantitative Benedict's test

      • Semi-quantitative Benedict's test to estimate reducing sugar concentration

    6. 2.1.6Non-reducing sugar hydrolysis test

      • Test for non-reducing sugars using acid hydrolysis and Benedict's solution

  2. 2.2 Carbohydrates and Lipids

    1. 2.2.1α-glucose and β-glucose rings

      • Draw ring forms of α-glucose and β-glucose

    2. 2.2.2Biological molecule terminology

      • Define: monomer, polymer, macromolecule, monosaccharide, disaccharide, polysaccharide

    3. 2.2.3Role of covalent bonds in forming polymers

      • Role of covalent bonds in forming polymers

    4. 2.2.4Reducing and non-reducing sugars

      • Identify reducing sugars (glucose, fructose, maltose) and non-reducing sugars (sucrose)

    5. 2.2.5Glycosidic bonds

      • Glycosidic bond formation by condensation and breakage by hydrolysis

    6. 2.2.6Molecular structure of polysaccharides

      • Molecular structure of polysaccharides: - Starch (amylose and amylopectin) - structure and function - Glycogen - structure and function - Cellulose - structure and role in plant cell walls

    7. 2.2.7Triglycerides

      • Triglycerides: non-polar hydrophobic molecules - Structure: fatty acids (saturated/unsaturated), glycerol, ester bonds - Functions in living organisms

    8. 2.2.8Phospholipids

      • Phospholipids: hydrophilic phosphate heads, hydrophobic fatty acid tails

  3. 2.3 Proteins

    1. 2.3.1Amino acids and peptide bonds

      • General structure of amino acids and peptide bond formation/breakage

    2. 2.3.2Protein structure levels

      • Protein structure levels: primary, secondary, tertiary, quaternary

    3. 2.3.3Interactions holding protein shape

      • Interactions holding protein shape: - Hydrophobic interactions - Hydrogen bonding - Ionic bonding - Covalent bonding (including disulfide bonds)

    4. 2.3.4Globular proteins

      • Globular proteins: soluble, physiological roles

    5. 2.3.5Fibrous proteins

      • Fibrous proteins: insoluble, structural roles

    6. 2.3.6Haemoglobin quaternary structure

      • Haemoglobin structure: quaternary structure with 2α-globin chains, 2β-globin chains, haem group

    7. 2.3.7Haemoglobin function

      • Haemoglobin function: importance of iron in haem group

    8. 2.3.8Collagen structure

      • Collagen structure and arrangement into collagen fibres

    9. 2.3.9Collagen structure and function

      • Relate collagen structure to function

  4. 2.4 Water

    1. 2.4.1Hydrogen bonding between water molecules

      • Hydrogen bonding between water molecules

    2. 2.4.2Properties and roles in living organisms

      • Properties and roles in living organisms: - Solvent action - High specific heat capacity - High latent heat of vaporisation