Proteins

Subdecks (1)

Cards (36)

  • protein’s monomer -> amino acid
  • amino acid are made up of H , N , C , O
  • NH2 is the amine group
  • COOH is the carboxyl group
  • R represents a variable side chain which is different for each of the 20 amino acids
  • Peptide bond - a condensation reaction between two amino acids
  • Dipeptides are formed by the condensation reaction of two amino acids
  • Polypeptides are formed by the condensation reaction of many amino acids
  • the general structure of a amino acid :
    • Carboxyl group ( COOH )
    • R variable
    • amine group ( NH2 )
  • Test for proteins in a sample :
    1. add equal volume of sodium hydroxide to a sample at room temperature
    2. add drops of dilute copper sulfate solution , swirl to mix
    3. POSITIVE RESULT : colour changes from blue to purple NEGATIVE RESULT : solution remains blue
  • there are 20 amino acids and they differ by side ' R ' group
  • condensation reaction forms peptide bond
  • dipeptide : 2 amino acids
  • polypeptide : 3 or more amino acids
  • two types of secondary protein structure
    • a helix
    • b pleated sheet
  • a helix :
    all N-H bonds on same side of protein chain
    spiral shape
    H-bonds parallel to helical axis
  • b-pleated sheet :
    N-H an C=O groups alternate from one side to the other
  • disulfide bridges : strong covalent S-S bonds between molecules of the amino acid cysteine
  • ionic bonds : relativley strong bonds between charged R groups
  • hydrogen bonds : numerous & easily broken
  • Globular proteins :
    spherical and compact
    involved in metabolic processes
  • fibrous proteins :
    • form long chains or fibres
    • insoluble in water
    • use for structure and support
  • enyzmes are biological catalysts
  • induced fit model of enzyme action :
    • shape of active site is not directly complementary to substrate and is flexible
  • lock and key : rigid shape of active site complimentary to only 1 substrate
  • competitive inhibitors:
    • similar shape to substrate , bind to active site
  • non-competitive inhibitors :
    • bind at allosteric binding site
  • structure of proteins is determined by the order and number amino acids, bonding present and the shape of the protein