This site is intended for healthcare professionals

Sign in
Go to /sign-in page

You can view 5 more pages before 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.

The content herein is provided for informational purposes and does not replace the need to apply professional clinical judgement when diagnosing or treating any medical condition. A licensed medical practitioner should be consulted for diagnosis and treatment of any and all medical conditions.

Connect

Copyright 2024 Oxbridge Solutions Limited, a subsidiary of OmniaMed Communications Limited. All rights reserved. Any distribution or duplication of the information contained herein is strictly prohibited. Oxbridge Solutions receives funding from advertising but maintains editorial independence.