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Structural modification (amino acids)

Last reviewed dd mmm yyyy. Last edited dd mmm yyyy

Authoring team

Amino acids can be modified in several ways:

  • phosphorylation at serine and threonine residues; one means of secondary messenger and hormonal activation
  • addition of carbohydrate groups to give proteoglycans:
    • usually bound to nitrogen or oxygen atom
    • may protect against proteolysis
    • role in membrane recognition
  • addition of lipid to give lipoprotein
  • formation of covalent bonds e.g.:
    • disulphide bridges between cysteine residues
    • peptide bonds between -C00H and -NH2 groups; the basis of polypeptide formation
  • formation of hydrogen bonds between hydrogen and oxygen atoms in adjacent amino acid residues
  • formation of van der Waals bonds between adjacent hydrophobic portions of 2 amino acids

These sorts of interaction determine the arrangement of higher levels of protein structure; hence, they have a vital role to play in protein function.

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