An introduction to NMR-based approaches for measuring protein dynamics

被引：391

作者：

Kleckner, Ian R. ^{[2
]}

Foster, Mark P. ^{[1
]}

机构：

[1] Ohio State Univ, Dept Biochem, Columbus, OH 43210 USA

[2] Ohio State Univ, Biophys Program, Columbus, OH 43210 USA

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS | 2011年 / 1814卷 / 08期

基金：

美国国家卫生研究院;

关键词：

Protein dynamics; Protein flexibility; NMR; RESIDUAL DIPOLAR COUPLINGS; NUCLEAR-MAGNETIC-RESONANCE; MODEL-FREE APPROACH; RELAXATION DISPERSION EXPERIMENTS; PROTON-EXCHANGE RATES; CHARACTERIZING CHEMICAL-EXCHANGE; TRANSIENT ENCOUNTER COMPLEXES; COUPLED EVOLUTION PERIODS; ISOTOPE LABELING METHODS; TEMPERATURE-DEPENDENCE;

D O I：

10.1016/j.bbapap.2010.10.012

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：

Proteins are inherently flexible at ambient temperature. At equilibrium, they are characterized by a set of conformations that undergo continuous exchange within a hierarchy of spatial and temporal scales ranging from nanometers to micrometers and femtoseconds to hours. Dynamic properties of proteins are essential for describing the structural bases of their biological functions including catalysis, binding, regulation and cellular structure. Nuclear magnetic resonance (NMR) spectroscopy represents a powerful technique for measuring these essential features of proteins. Here we provide an introduction to NMR-based approaches for studying protein dynamics, highlighting eight distinct methods with recent examples, contextualized within a common experimental and analytical framework. The selected methods are (1) Real-time NMR, (2) Exchange spectroscopy, (3) Lineshape analysis, (4) CPMG relaxation dispersion, (5) Rotating frame relaxation dispersion, (6) Nuclear spin relaxation, (7) Residual dipolar coupling, (8) Paramagnetic relaxation enhancement This article is part of a Special Issue entitled: Protein Dynamics: Experimental and Computational Approaches. (C) 2010 Elsevier B.V. All rights reserved.

引用

页码：942 / 968

页数：27

共 201 条

[21] How do proteins interact? [J].

Boehr, David D. ;

Wright, Peter E. .

SCIENCE, 2008, 320 (5882) :1429-1430

[22] The dynamic energy landscape of dihydrofolate reductase catalysis [J].

Boehr, David D. ;

McElheny, Dan ;

Dyson, H. Jane ;

Wright, Peter E. .

SCIENCE, 2006, 313 (5793) :1638-1642

[23] An NMR perspective on enzyme dynamics [J].

Boehr, David D. ;

Dyson, H. Jane ;

Wright, Peter E. .

CHEMICAL REVIEWS, 2006, 106 (08) :3055-3079

[24] Millisecond timescale fluctuations in dihydrofolate reductase are exquisitely sensitive to the bound ligands [J].

Boehr, David D. ;

McElheny, Dan ;

Dyson, H. Jane ;

Wright, Peter E. .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2010, 107 (04) :1373-1378

[25] The role of dynamic conformational ensembles in biomolecular recognition [J].

Boehr, David D. ;

Nussinov, Ruth ;

Wright, Peter E. .

NATURE CHEMICAL BIOLOGY, 2009, 5 (11) :789-796

[26]

Box G.E.P., 2005, Statistics for Experimenters. Design, Innovation, and Discovery, V2

[27] Temperature dependence of intramolecular dynamics of the basic leucine zipper of GCN4: Implications for the entropy of association with DNA [J].

Bracken, C ;

Carr, PA ;

Cavanagh, J ;

Palmer, AG .

JOURNAL OF MOLECULAR BIOLOGY, 1999, 285 (05) :2133-2146

[28] NMR-STUDY OF HISTIDINE RESIDUES OF S-PEPTIDE AND S-PROTEIN AND KINETICS OF H-1-H-2 EXCHANGE OF RIBONUCLEASE-A [J].

BRADBURY, JH ;

CROMPTON, MW ;

TEH, JS .

EUROPEAN JOURNAL OF BIOCHEMISTRY, 1977, 81 (02) :411-422

[29] Residue-specific NH exchange rates studied by NMR diffusion experiments [J].

Brand, Torsten ;

Cabrita, Eurico J. ;

Morris, Gareth A. ;

Guenther, Robert ;

Hofmann, Hans-Jorg ;

Berger, Stefan .

JOURNAL OF MAGNETIC RESONANCE, 2007, 187 (01) :97-104

[30] Differential Responses of the Backbone and Side-Chain Conformational Dynamics in FKBP12 upon Binding the Transition-State Analog FK506: Implications for Transition-State Stabilization and Target Protein Recognition [J].

Brath, Ulrika ;

Akke, Mikael .

JOURNAL OF MOLECULAR BIOLOGY, 2009, 387 (01) :233-244

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