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Protein deamidation is a post-translational modification in which the side chain amide group of a glutamine or asparagine residue is transformed into an acidic carboxylate group (Geiger et al., 1987). Non-enzymatic deamidation of asparagine is faster than of glutamine and hence presents higher physiological significance (Robinson et al., 2001), being involved in processes such as apoptosis, brain development and aging (Reissner et al., 2003). Deamidation often (Reissner et al., 2003), but not always, leads to loss of protein function.
(Geiger et al., 1987) Deamidation, isomerization, and racemization at asparaginyl and aspartyl residues in peptides. Succinimide-linked reactions that contribute to protein degradation. Biol Chem.
(Robinson et al., 2001) Molecular clocks. Proc Natl Acad Sci U S A.
(Reissner et al., 2003) Deamidation and isoaspartate formation in proteins: unwanted alterations or surreptitious signals? Cell Mol Life Sci.
(Lorenzo et al., 2015) Prediction of Spontaneous Protein Deamidation from Sequence-Derived Secondary Intrinsic Disorder. PLoS One.