Chemical modification is the change of biomolecular structure and function due to the addition or removal of modifying elements.
Chemical modifiers on compounds that can be used as drugs can also be used to attempt to increase the shelf life of the product or extend its function.
Common chemical modifications include phosphorylation, glycosylation, ubiquitination, methylation, lipidation, and proteolysis.
[1] Although we will cover each type of chemical modification singularly, they can often work in conjunction with each other to modify the protein.
[4] Phosphatases can act as a regulator and editor of cellular signaling pathways forming transient protein-protein interactions.
[8] Many proteins that are glycosylated are often found on cell surfaces and play a large role in determining blood type.
[9] The degradation function of ubiquitin is the most well-understood as it has been linked to the NF-𝜿B signaling pathway for triggering inflammation.
[1] It is also often used by histone proteins to allow certain regions of the genome to wind and unwind and become accessible for transcription.
There are four common types of lipidation: GPI anchors, N-terminal myristoylation, S-myristoylation, and S-prenylation.
Oftentimes, peptide bonds are stable in typical physiological conditions and may need enzymes called proteases to assist in breaking polypeptides into smaller components.