Secondary Structure and Protein Deamidation
- 1 January 1999
- journal article
- review article
- Published by American Geophysical Union (AGU) in Journal of Pharmaceutical Sciences
- Vol. 88 (1) , 8-13
- https://doi.org/10.1021/js9802493
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.Keywords
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