This site is intended for healthcare professionals

account_circleSign in
Go to /sign-in page

You can view 5 more pages without signing in

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.

Related pages

Create an account to add page annotations

Create a free account

Annotations allow you to add information to this page that would be handy to have on hand during a consultation. E.g. a website or number. This information will always show when you visit this page.