PROTEIN STABILITY AND ELECTROSTATIC INTERACTIONS BETWEEN SOLVENT EXPOSED CHARGED SIDE-CHAINS

被引：108

作者：

AKKE, M ^{[1
]}

FORSEN, S ^{[1
]}

机构：

[1] UNIV LUND,DEPT PHYS CHEM,POB 124,S-22100 LUND,SWEDEN

来源：

PROTEINS-STRUCTURE FUNCTION AND GENETICS | 1990年 / 8卷 / 01期

关键词：

calbindin D[!sub]9k[!/sub; increased stability; site‐directed mutagenesis; urea induced unfolding;

D O I：

10.1002/prot.340080106

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：

To investigate the contribution to protein stability of electrostatic interactions between charged surface residues, we have studied the effect of substituting three negatively charged solvent exposed residues with their side‐chain amide analogs in bovine calbindin D9k—a small (Mr 8,500) globular protein of the calmodulin superfamily. The free energy of urea‐induced unfolding for the wildtype and seven mutant proteins has been measured. The mutant proteins have increased stability towards unfolding relative to the wildtype. The experimental results correlate reasonably well with theoretically calculated relative free energies of unfolding and show that electrostatic interactions between charges on the surface of a protein can have significant effects on protein stability. Copyright © 1990 Wiley‐Liss, Inc.

引用

页码：23 / 29

页数：7

共 33 条

[1] A MOLECULAR-DYNAMICS SIMULATION OF BOVINE CALBINDIN D9K - MOLECULAR-STRUCTURE AND DYNAMICS [J].