•  Primary protein structure. Properties of peptide bonds: double-bond character, planar, charge, configuration. Influence of primary structure on function of proteins (on an example of hereditary infringements of primary structure and functions of haemoglobins A)
  •  Secondary structure: α-helix and β-sheets. Obstacles to formation of certain kinds of secondary structure. Supersecondary structure of proteins: helix-turn-helix, leucine zipper, zing finger.
  •  Tertiary structure of proteins. Types of interactions between side chains of amino acids residues that form tertiary structure. Formation of tertiary structure of proteins from elements of the secondary structure, steady combinations of elements of secondary structure, structural motives. The shape of proteins as result of the tertiary structural organization.
  •  Physico-chemical properties of proteins. Isoelectric point (pI). Molecular mass, shape and charge of molecules.
  •  Factors determining the solubility of proteins; reversible and irreversible sedimentation.
  •  Denaturation and renaturation of proteins.
  •  Fractional sedimentation of proteins from a sample of blood plasma.
  •  Precipitation of proteins using organic acids, alcohol and acetone.
Last modified: Monday, 17 February 2014, 9:55 AM