DISULFIDE CROSS-LINKS TO PROBE THE STRUCTURE AND FLEXIBILITY OF A DESIGNED 4-HELIX BUNDLE PROTEIN

被引：24

作者：

REGAN, L ^{[1
]}

ROCKWELL, A ^{[1
]}

WASSERMAN, Z ^{[1
]}

DEGRADO, W ^{[1
]}

机构：

[1] DUPONT CO INC, EXPTL STN, WILMINGTON, DE 19880 USA

来源：

PROTEIN SCIENCE | 1994年 / 3卷 / 12期

关键词：

DISULFIDE CROSS-LINKS; DISULFIDE REDOX POTENTIAL; 4-HELIX BUNDLE PROTEIN; PROTEIN DESIGN; PROTEIN STABILITY;

D O I：

10.1002/pro.5560031225

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：

The introduction of disulfide crosslinks is a generally useful method by which to identify regions of a protein that are close together in space, Here we describe the use of disulfide crosslinks to investigate the structure and flexibility of a family of designed 4-helix bundle proteins. The results of these analyses lend support to our working model of the proteins' structure and suggest that the proteins have limited main-chain flexibility.

引用

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页码：2419 / 2427

页数：9

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