Multi-Timescale Conformational Dynamics of the SH3 Domain of CD2-Associated Protein using NMR Spectroscopy and Accelerated Molecular Dynamics

被引：27

作者：

Salmon, Loic ^{[1
]}

Pierce, Levi ^{[2
]}

Grimm, Alexander ^{[1
]}

Roldan, Jose-Luis Ortega ^{[4
]}

Mollica, Luca ^{[1
]}

Jensen, Malene Ringkjobing ^{[1
]}

van Nuland, Nico ^{[3
]}

Markwick, Phineus R. L. ^{[2
]}

McCammon, J. Andrew ^{[2
]}

Blackledge, Martin ^{[1
]}

机构：

[1] CNRS CEA UJF, Inst Biol Struct Jean Pierre Ebel, UMR 5075, F-38027 Grenoble, France

[2] UCSD, Dept Chem & Biochem, San Diego Howard Hughes Med Inst, La Jolla, CA USA

[3] Vrije Univ Brussel, Brussels, Belgium

[4] Univ Oxford, Dept Biochem, Oxford OX1 3QU, England

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2012年 / 51卷 / 25期

关键词：

molecular recognition; NMR spectroscopy; protein dynamics; residual dipolar couplings; spin relaxation; RESIDUAL DIPOLAR COUPLINGS; MULTIPLE ALIGNMENT MEDIA; BIOLOGICAL MACROMOLECULES; BIOMOLECULAR STRUCTURE; BACKBONE STRUCTURE; MOTIONS; UBIQUITIN; ENSEMBLE; CD2AP; RELAXATION;

D O I：

10.1002/anie.201202026

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

An extensive set of experimental NMR residual dipolar couplings (RDCs) has been used to determine the conformational behavior of the SH3 domain of CD2-associated protein. Analytical descriptions of the local dynamics were compared to restraint-free accelerated molecular dynamics simulation, providing a convergent and comprehensive description of conformational fluctuations on picosecond to millisecond timescales. Copyright © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

引用

页码：6103 / 6106

页数：4

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