Dynamic activation of protein function: A view emerging from NMR spectroscopy

被引：283

作者：

Wand, AJ ^{[1
]}

机构：

[1] Univ Penn, Johnson Res Fdn, Philadelphia, PA 19104 USA

[2] Univ Penn, Dept Biochem & Biophys, Philadelphia, PA 19104 USA

来源：

NATURE STRUCTURAL BIOLOGY | 2001年 / 8卷 / 11期

基金：

美国国家卫生研究院;

关键词：

D O I：

10.1038/nsb1101-926

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：

Recent developments in solution NMR methods have allowed for an unprecedented view of protein dynamics. Current insights into the nature of protein dynamics and their potential influence on protein structure, stability and function are reviewed. Particular emphasis is placed on the potential of fast side chain motion to report on the residual conformational entropy of proteins and how this entropy can enter into both the thermodynamic and kinetic aspects of protein function.

引用

收藏

页码：926 / 931

页数：6

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