Cards (8)

  • Proteins are sequences of amino acids joined by peptide links.
    • When 2 amino acids join together, it is a dipeptide.
    • When 3 amino acids join together, it is a tripeptide.
    • When many amino acids join together, it is a protein or polypeptide.
  • Formation of a protein= Condensation reaction= Two amino acids are joined together, linked through a peptide link, one molecule of water is released.
    Destruction of a protein= Hydrolysis reaction= Peptide link is broken between two amino acids, requires one molecule of water.
    A) Amino acid
    B) Amino acid
    C) Condensation
    D) Hydrolysis
    E) Dipeptide
    F) Peptide link
  • 2 different amino acids can join to form 2 different dipeptides:
  • Proteins, polypeptides, dipeptides and tripeptides can all be hydrolysed back into their  constituent amino acids. This can be done using an acid or alkaline catalyst.
  • Acidic hydrolysis:
    • Conditions - 6 mol dm-3 HCl, reflux 24 hours:
    • Produces an alkyl ammonium salt.
  • Alkali hydrolysis:
    • Conditions - Solution of aqueous NaOH, heated above 100 degrees.
    • Produces an carboxylate salt.
  • Structure of proteins:
    • Primary structure - Sequence of amino acids joined by peptide links.
    • Secondary structure - Hydrogen bonds form between peptide links. This causes the amino acid sequence of coil, into an alpha helix, or fold, into a beta-pleated sheet.
    • Tertiary structure- The secondary structure folds and coils on itself to give a 3-dimensional structure. Additional bonds and intermolecular forces hold the polypeptide or protein in this shape.
  • Additional bonds and intermolecular forces:
    • Van der Waals’ forces of attraction, these form between the alkyl R side groups
    • Hydrogen bonds, these form between OH / NH / C=O in the R side groups and the main chain. They stabilise and provide support for the secondary structure.
    • Ionic bonds, form between COO- and NH3+ in the R side group.
    • Disulphide bonds (sulphur – sulphur bonds), formed between cysteine residues. They stabilise the protein.