To charge or not to charge?

被引：184

作者：

Sanchez-Ruiz, JM ^{[1
]}

Makhatadze, GI

机构：

[1] Univ Granada, Dept Chem Phys, Fac Sci, E-18071 Granada, Spain

[2] Univ Granada, Inst Biotechnol, E-18071 Granada, Spain

[3] Penn State Univ, Coll Med, Dept Biochem & Mol Biol, Hershey, PA 17033 USA

来源：

TRENDS IN BIOTECHNOLOGY | 2001年 / 19卷 / 04期

关键词：

D O I：

10.1016/S0167-7799(00)01548-1

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

The ability to engineer proteins with increased thermostability will profoundly broaden their practical applications. Recent experimental results show that optimization of charge-charge interactions on the surface of proteins can be a useful strategy in the design of thermostable enzymes. Results also indicate a possibility that such optimized interactions provide structural determinants for enhanced stability of proteins from thermophilic organisms. In this article, the general strategy for design of thermostable proteins and perspectives for future studies are discussed.

引用

页码：132 / 135

页数：4

共 31 条

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