PTM Peptides

Post-translational modification (PTM) is the covalent and generally enzymatic modification of proteins following biosynthesis. Proteins are initially synthesized as polypeptide chains, which then undergo modification to form the active protein. PTMs are important in cell signalling, such as when prohormones are converted to hormones.
Post-translational modifications can occur on the amino acid side chains or at the C- or N- terminus.   Sites that undergo post-translational modification are generally those that have a reactive functional group – the hydroxyl groups of serine, threonine and tyrosine, the amine groups of lysine, arginine, and histidine, and the thiolate anion of cysteine and the carboxylates of aspartate and glutamate. The amide of asparagine is sometimes attached to glycans.
Phosphorylation is a very common mechanism for regulating the activity of enzymes and is the most common post-translational modification.   There are very many types of PTM that can occur but the most common are phosphorylation, acetylation, N-linked glycosylation, amidation, hydroxylation, methylation, O-linked glycosylation, ubiquitylation and sulphation.  Attachment of lipids often targets a protein or part of a protein attached to the cell membrane.

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