Biological molecules

Cards (76)

  • Biological molecules
    • Carbohydrates
    • Lipids
    • Proteins
    • Nucleic Acids
  • Carbohydrates
    Molecules consisting only of carbon, hydrogen and oxygen. They are long chains of sugar units called saccharides.
  • Types of saccharides
    • Monosaccharides
    • Disaccharides
    • Polysaccharides
  • Monosaccharide
    Single sugar monomer
  • Disaccharide
    Two monosaccharides
  • Polysaccharide
    Many monosaccharides
  • Glycosidic bonds

    Bonds formed in condensation reactions that join monosaccharides to form disaccharides and polysaccharides
  • Glucose
    A monosaccharide containing six carbon atoms, the main substrate for respiration
  • Glucose isomers
    • Alpha glucose
    • Beta glucose
  • Ribose
    A monosaccharide containing five carbon atoms, a component of RNA
  • Deoxyribose
    An isomer of ribose that lacks the OH group on the second carbon of the sugar ring, a component of DNA
  • Polysaccharides
    • Glycogen
    • Starch
    • Cellulose
  • Glycogen
    The main energy storage molecule in animals, formed from many molecules of alpha glucose joined by 1,4 and 1,6 glycosidic bonds, has a large number of side branches
  • Starch
    The energy storage molecule in plants, a mixture of amylose (unbranched chain of glucose molecules joined by 1,4 glycosidic bonds) and amylopectin (branched molecule of glucose molecules joined by 1,4 and 1,6 glycosidic bonds)
  • Cellulose
    A component of plant cell walls, composed of long, unbranched chains of beta glucose monomers joined by 1,4 glycosidic bonds, forms microfibrils that provide structural support
  • Lipids
    Biological molecules only soluble in organic solvents
  • Types of lipids
    • Saturated lipids
    • Unsaturated lipids
  • Saturated lipids
    Lipids that only contain carbon-carbon single bonds, found in animal fats
  • Unsaturated lipids
    Lipids that contain carbon-carbon double bonds, found in plants
  • Intermolecular forces
    Weaker in unsaturated lipids, resulting in a lower melting point
  • Triglycerides
    Lipids made of one molecule of glycerol and three fatty acids joined by ester bonds formed in condensation reactions, used as energy reserves
  • Phospholipids
    Lipids with one fatty acid substituted by a phosphate-containing group, form a bilayer in the cell membrane with hydrophilic heads and hydrophobic tails
  • Amino acids
    The monomers from which proteins are made, contain an amino group, a carboxyl group, and a variable R group that determines the chemical properties
  • Peptide bonds
    Bonds formed in condensation reactions that join amino acids to form dipeptides and polypeptides
  • Levels of protein structure
    • Primary
    • Secondary
    • Tertiary
    • Quaternary
  • Primary structure
    The linear sequence of amino acids in the polypeptide chain, held together by peptide bonds
  • Secondary structure
    The folding of the polypeptide chain into alpha helices or beta pleated sheets, held together by hydrogen bonds
  • Tertiary structure

    The 3D folding of the secondary structure into a complex shape, determined by hydrogen bonding, ionic bonding, and disulfide bridges
  • Quaternary structure
    The 3D arrangement of more than one polypeptide
  • Types of proteins
    • Fibrous
    • Globular
  • Fibrous proteins
    • Long parallel polypeptides, very little tertiary/quaternary structure, occasional cross-linkages, insoluble, used for structural purposes
  • Globular proteins

    • Complex tertiary/quaternary structures, form colloids in water, many uses e.g. hormones, antibodies
  • Ionic bonding
    Salt bridges, form between oppositely charged groups on the R groups
  • Disulphide bridges

    Covalent bonds between sulphur atoms in cysteine
  • Not all proteins have all levels of structure
  • Types of proteins
    • Fibrous
    • Globular
  • Fibrous proteins

    • Long parallel polypeptides
    • Very little tertiary/quaternary structure - mainly secondary structure
    • Occasional cross-linkages which form microfibrils for tensile strength
    • Insoluble
    • Used for structural purposes
  • Globular proteins

    • Complex tertiary/quaternary structures
    • Form colloids in water
    • Many uses e.g. hormones, antibodies
  • Fibrous protein

    • Collagen
  • Collagen
    • High tensile strength due to large number of hydrogen bonds in the structure
    • Molecules are made up of three distinct α-chains which form a triple gamma helix
    • Multiple of these helices link together to form fibrils and strong collagen fibres
    • Forms the structure of bones, cartilage and connective tissue
    • Main component of tendons which connect muscles to bones