Cards (14)

  • globular proteins
    compact
    spherical
    soluble in water -> orientation of hydro-interactions
    easily transported and involved in metabolic reactions
    folding into specific shapes -> enzymes and active sites, and receptors for antigens
  • conjugated protein
    contain a prosthetic group
  • haemoglobin
    carries oxygen as oxyhaemoglobin
    quaternary structure -> 4 polypeptide chains
    2 a-globin and 2 b-globin
    4 globin chains held by disulfide bonds
    haem group (fe2+) holds oxygen
  • function of haemoglobin
    transport oxygen around the body
    soluble -> more efficient travel in the blood than oxygen by itself
    each oxygen binds and alters the quaternary structure making the next molecule easier to bind
  • insulin
    produced by b-cells in the pancreas
    control of blood glucose
    two polypeptide chains held by disulfide bonds
    specific structure to membrane receptors
  • pepsin
    enzyme
    suited to acidic conditions in the stomach
  • fibrous proteins
    long polypeptide chains with cross links between chains due to hydrogen bonding
    insoluble due to the presence of increased hydrophobic R groups
    highly repetitive amino acid sequence -> organised structure
  • (f) collagen
    flexible -> connective tissues
    many hydrogen bonds -> increase tensile strength
    insoluble -> high length increases time taken to dissolve
    present in artery walls to withstand pressure
  • (f) keratin
    strong
    large amounts of the amino acid cysteine which increases the amount of disulfide bonds
    found in finger nails and hair
  • (f) elastin
    connective tissue
    blood vessels -> stretch and recoil to each pulse response
  • primary structure
    sequence of amino acids with peptide bonds between them
  • secondary structure
    beta pleated sheet or alpha helix
    hydrogen bonds
  • tertiary structure
    ionic and disulfide bonds
    hydrophobic and hydrophillic interactions
  • structure of collagen
    peptide bonds between amino acids
    every third amino acid is glycine
    coils into a helix
    three polypeptide chains
    hydrogen bonds between the chains
    forms fibrils