Protein dynamic studies move to a new time slot

被引：15

作者：

Cavanagh, J ^{[1
]}

Venters, RA

机构：

[1] N Carolina State Univ, Dept Mol & Struct Biochem, Raleigh, NC 27695 USA

[2] Duke Univ, NMR Ctr, Durham, NC 27710 USA

来源：

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

关键词：

D O I：

10.1038/nsb1101-912

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：

Many proteins frequently undergo structural rearrangement to complete their functions. Ligand entry and binding are often associated with some degree of localized disorder. Indeed, low populations of disordered excited states may help drive such processes. Characterization of these states is vital to understanding the mechanisms of many biological functions.

引用

页码：912 / 914

页数：3

共 33 条

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