NMR methods for characterizing microsecond to millisecond dynamics in recognition and catalysis

被引：111
作者：
Akke, M [1 ]
机构：
[1] Lund Univ, Dept Biophys Chem, SE-22100 Lund, Sweden
来源：
CURRENT OPINION IN STRUCTURAL BIOLOGY | 2002年 / 12卷 / 05期
关键词：
D O I：
10.1016/S0959-440X(02)00369-X
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：
During the past two years, significant advances have been made in the development of NMR methods for studying biomolecular dynamics on the microsecond to millisecond timescale. Applications of these methods to biologically relevant systems have provided compelling evidence that, in many cases, conformational dynamics on these timescales govern the rates of biomolecular recognition and catalysis.
引用
收藏
页码：642 / 647
页数：6
相关论文
共 65 条
[1]   Pervasive conformational fluctuations on microsecond time scales in a fibronectin type III domain [J].
Akke, M ;
Liu, J ;
Cavanagh, J ;
Erickson, HP ;
Palmer, AG .
NATURE STRUCTURAL BIOLOGY, 1998, 5 (01) :55-59
[2]   13C spin relaxation measurements in RNA:: Sensitivity and resolution improvement using spin-state selective correlation experiments [J].
Boisbouvier, J ;
Brutscher, B ;
Simorre, JP ;
Marion, D .
JOURNAL OF BIOMOLECULAR NMR, 1999, 14 (03) :241-252
[3]   Solution structure and dynamics of yeast elongin C in complex with a von Hippel-Lindau peptide [J].
Botuyan, MV ;
Mer, G ;
Yi, GS ;
Koth, CM ;
Case, DA ;
Edwards, AM ;
Chazin, WJ ;
Arrowsmith, CH .
JOURNAL OF MOLECULAR BIOLOGY, 2001, 312 (01) :177-186
[4]   Chemical basis for enzyme catalysis [J].
Bruice, TC ;
Benkovic, SJ .
BIOCHEMISTRY, 2000, 39 (21) :6267-6274
[5]   Evidence for flexibility in the function of ribonuclease A [J].
Cole, R ;
Loria, JP .
BIOCHEMISTRY, 2002, 41 (19) :6072-6081
[6]   Long timescale simulations [J].
Daggett, V .
CURRENT OPINION IN STRUCTURAL BIOLOGY, 2000, 10 (02) :160-164
[7]   DIRECT MEASUREMENTS OF THE DISSOCIATION-RATE CONSTANT FOR INHIBITOR-ENZYME COMPLEXES VIA THE T-1-RHO AND T-2 (CPMG) METHODS [J].
DAVIS, DG ;
PERLMAN, ME ;
LONDON, RE .
JOURNAL OF MAGNETIC RESONANCE SERIES B, 1994, 104 (03) :266-275
[8]   Enzyme dynamics during catalysis [J].
Eisenmesser, EZ ;
Bosco, DA ;
Akke, M ;
Kern, D .
SCIENCE, 2002, 295 (5559) :1520-1523
[9]   Dynamics of the transition between open and closed conformations in a calmodulin C-terminal domain mutant [J].
Evenäs, J ;
Malmendal, A ;
Akke, M .
STRUCTURE, 2001, 9 (03) :185-195
[10]   Millisecond-timescale motions contribute to the function of the bacterial response regulator protein Spo0F [J].
Feher, VA ;
Cavanagh, J .
NATURE, 1999, 400 (6741) :289-293
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