Deamidation is a post-translational modification that occurs in proteins, in which the amide group of the amino acid Asparagine (Asn) is replaced by an amine group. It is a common mechanism of protein turnover and can significantly alter protein function. Asn can be found in both intracellular and extracellular proteins, and in both natural and synthetic analogs. Deamidation can be induced by pH, temperature, or dehydration, as well as chemical agents such as glutaraldehyde, transglutaminase, and intermolecular nucleophiles. This process can have a significant impact on the biological activity and stability of the affected proteins. Deamidation is therefore essential to understand when developing biotherapeutics, as it helps to ensure the safety and efficacy of the drug. In addition, deamidation can be used to characterize and quantify proteins, by taking advantage of the distinct changes in physical and chemical properties that it causes.

From: International Journal of Amino Acids

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Editor: Julia Piccoli, University of Sao Paulo-UNESP
Publication Type: Open Access Journal
Description: International Journal of Amino Acids encourages author to submit manuscripts to the journal for evaluation, from all fields of amino acid and protein research: analysis, separation, synthesis, biosynthesis, cross linking amino acids, racemization/enantiomers, modification of amino acids as phosphorylation, methylation, acetylation of amino acids.