Influence of backbone conformation on protein aggregation

被引：49

作者：

Srisailam, S ^{[1
]}

Kumar, TKS ^{[1
]}

Srimathi, T ^{[1
]}

Yu, C ^{[1
]}

机构：

[1] Natl Tsing Hua Univ, Dept Chem, Hsinchu, Taiwan

来源：

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 2002年 / 124卷 / 09期

关键词：

D O I：

10.1021/ja012070r

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Effect(s) of organic solvents on an all beta-sheet protein are investigated to understand the influence of backbone conformation on protein aggregation. Results obtained in the present study reveal that protein aggregation is accompanied by the formation of non-native beta-sheet conformation. In contrast, induction of non-native helical segments in the protein is found to inhibit aggregation. The differential effects of the secondary structures on protein aggregation are proposed to stem from the disparity in the nature of the hydrogen bonds and packing of the side chains of hydrophobic residues in the beta-sheet and a-helix conformation. In our opinion, the results of the present study provide useful hints to develop methods to alleviate the problems of both in vitro and in vivo protein aggregation.

引用

页码：1884 / 1888

页数：5

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