Characterization of the dynamics of biomacromolecules using rotating-frame spin relaxation NMR spectroscopy

被引：266

作者：

Palmer, Arthur G., III ^{[1
]}

Massi, Francesca ^{[1
]}

机构：

[1] Columbia Univ, Dept Biochem & Mol Biophys, New York, NY 10032 USA

来源：

CHEMICAL REVIEWS | 2006年 / 106卷 / 05期

关键词：

D O I：

10.1021/cr0404287

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Line shape analysis and Carr-Purcell-Meiboom-Gill (CPMG) relaxation have been more commonly utilized than R1ρ relaxation dispersion. However, recent theoretical and experimental advances have made R1ρ measurements much more powerful for characterizing microsecond to millisecond conformational dynamics and chemical kinetics in proteins and other biomacromolecules. The number of applications that use R1ρ techniques is increasing, and new insights are already emerging about dynamic events in folding, recognition, and catalysis. Overall, these developments open exciting new vistas for experimental investigations of the linkage between structure and dynamics in the function of biomacromolecules.

引用

页码：1700 / 1719

页数：20

共 80 条

[1] A Markov model for relaxation and exchange in NMR spectroscopy [J].

Abergel, D ;

Palmer, AG .

JOURNAL OF PHYSICAL CHEMISTRY B, 2005, 109 (11) :4837-4844

[2] Approximate solutions of the Bloch-McConnell equations for two-site chemical exchange [J].

Abergel, D ;

Palmer, AG .

CHEMPHYSCHEM, 2004, 5 (06) :787-793

[3] On the use of the stochastic Liouville equation in nuclear magnetic resonance:: Application to R1ρ relaxation in the presence of exchange [J].

Abergel, D ;

Palmer, AG .

CONCEPTS IN MAGNETIC RESONANCE PART A, 2003, 19A (02) :134-148

[4]

Abragam A., 2002, PRINCIPLES NUCL MAGN

[5]

Abramowitz M., 1974, HDB MATH FUNCTIONS F

[6] Monitoring macromolecular motions on microsecond to millisecond time scales by R(1)rho-R(1) constant relaxation time NMR spectroscopy [J].

Akke, M ;

Palmer, AG .

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1996, 118 (04) :911-912

[7]

[Anonymous], 2018, Protein nmr spectroscopy: principles and practice

[8] Multiple time scale backbone dynamics of homologous thermophilic and mesophilic ribonuclease HI enzymes [J].

Butterwick, JA ;

Loria, JP ;

Astrof, NS ;

Kroenke, CD ;

Cole, R ;

Rance, M ;

Palmer, AG .

JOURNAL OF MOLECULAR BIOLOGY, 2004, 339 (04) :855-871

[9] Temperature-dependence properties as studied by of protein hydrogen bond high-resolution NMR [J].

Cordier, F ;

Grzesiek, S .

JOURNAL OF MOLECULAR BIOLOGY, 2002, 317 (05) :739-752

[10] SECONDARY AND TERTIARY STRUCTURAL EFFECTS ON PROTEIN NMR CHEMICAL-SHIFTS - AN ABINITIO APPROACH [J].

DEDIOS, AC ;

PEARSON, JG ;

OLDFIELD, E .

SCIENCE, 1993, 260 (5113) :1491-1496

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