Secondary Structure and Protein Deamidation

The deamidation reactions of asparagine residues in α‐helical and β‐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 β‐sheet structures on asparagine stability is unclear, although simple considerations suggest a stabilization in this environment also.