Protein deamidation converts an amide-bearing side chain, commonly asparagine or glutamine, into a carboxyl-containing product. It can occur spontaneously or through catalysis and can alter charge, structure or molecular interactions. Some asparagine reactions also produce an altered backbone linkage, making the product chemically more complex than a simple residue replacement. Sample handling and elapsed time can therefore affect the observed modification pattern. [ref]
Molecular Biology of the Cell, 4th edition by Bruce Alberts and others. Chapter 3, Proteins: covalent modification and molecular properties
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