Characterizing weak protein-protein complexes by NMR residual dipolar couplings

被引：6

作者：

Jensen, Malene Ringkjobing ^{[1
]}

Ortega-Roldan, Jose-Luis ^{[2
]}

Salmon, Loic ^{[1
]}

van Nuland, Nico ^{[3
]}

Blackledge, Martin ^{[1
]}

机构：

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

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

[3] Vrije Univ Brussel, VIB Dept Mol & Cellular Interact, B-1050 Brussels, Belgium

来源：

EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS | 2011年 / 40卷 / 12期

关键词：

NMR; Interaction; Protein; Dynamics; Structure; Complex; ORIENTATIONAL CONSTRAINTS; BACKBONE MOTION; ORIENTED MEDIA; CYTOCHROME-C; SH3; DOMAINS; ALIGNMENT; UBIQUITIN; DYNAMICS; MACROMOLECULES; RECOGNITION;

D O I：

10.1007/s00249-011-0720-5

中图分类号：

Q6 [生物物理学];

学科分类号：

071011 ;

摘要：

Protein-protein interactions occur with a wide range of affinities from tight complexes characterized by femtomolar dissociation constants to weak, and more transient, complexes of millimolar affinity. Many of the weak and transiently formed protein-protein complexes have escaped characterization due to the difficulties in obtaining experimental parameters that report on the complexes alone without contributions from the unbound, free proteins. Here, we review recent developments for characterizing the structures of weak protein-protein complexes using nuclear magnetic resonance spectroscopy with special emphasis on the utility of residual dipolar couplings.

引用

页码：1371 / 1381

页数：11

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