Electrostatic and hydrophobic interactions play a major role in the stability and refolding of halophilic proteins

被引：25

作者：

Arakawa, T

Tokunaga, M

机构：

[1] Alliance Protein Labs, Thousand Oaks, CA 91360 USA

[2] Kagoshima Univ, Fac Agr, Kagoshima 8900065, Japan

来源：

PROTEIN AND PEPTIDE LETTERS | 2004年 / 11卷 / 02期

关键词：

halophilic; salt; nucleoside diphosphate kinase; refolding; charge shielding;

D O I：

10.2174/0929866043478220

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

In general, halophilic proteins are stable only in the presence of salts at high concentrations. Not only is high salt concentration important for structural stability of halophilic proteins, but also refolding of a denatured halophilic protein requires high salt concentration. This review summarizes the importance of electrostatic charge shielding and hydrophobic interactions in the stability and refolding of halophilic proteins.

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页码：125 / 132

页数：8

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