Large-scale shape changes in proteins and macromolecular complexes

被引：46

作者：

Wall, ME ^{[1
]}

Gallagher, SC ^{[1
]}

Trewhella, J ^{[1
]}

机构：

[1] Los Alamos Natl Lab, Biosci Div, Los Alamos, NM 87545 USA

来源：

ANNUAL REVIEW OF PHYSICAL CHEMISTRY | 2000年 / 51卷

关键词：

protein dynamics; conformational change; small-angle X-ray and neutron scattering; enzyme activation; kinase regulation;

D O I：

10.1146/annurev.physchem.51.1.355

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

Proteins and RNA undergo intricate motions as they carry out functions in biological systems. These motions frequently entail large-scale conformational changes that induce changes in the surface structure, or shape, of a molecule. This review describes the experimental characterization of large-scale shape changes in proteins and macromolecular complexes and the effects of such changes on macromolecular behavior. We describe several important results that have been obtained by using small-angle scattering, which is emerging as a powerful technique for determining macromolecular shapes and elucidating the quaternary structure of macromolecular assemblies.

引用

页码：355 / 380

页数：26

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