Secondary structure and protein deamidation

被引：101

作者：

Xie, ML ^{[1
]}

Schowen, RL ^{[1
]}

机构：

[1] Univ Kansas, Dept Pharmaceut Chem, Simons Lab Higuchi Biosci Ctr, Lawrence, KS 66047 USA

来源：

JOURNAL OF PHARMACEUTICAL SCIENCES | 1999年 / 88卷 / 01期

关键词：

D O I：

10.1021/js9802493

中图分类号：

R914 [药物化学];

学科分类号：

100701 ;

摘要：

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.

引用

页码：8 / 13

页数：6

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