Secondary Structure and Protein Deamidation
Journal of Pharmaceutical Sciences1999Vol. 88(1), pp. 8–13
Citations Over TimeTop 11% of 1999 papers
Abstract
The deamidation reactions of asparagine residues in alpha-helical and beta-turn secondary structural environments of peptides and proteins are reviewed. Both kinds of secondary structure tend to stabilize asparagine residues against deamidation, although the effects are not large. The effect of beta-sheet structures on asparagine stability is unclear, although simple considerations suggest a stabilization in this environment also.
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