Model-free approach beyond the borders of its applicability

被引:47
作者
Korzhnev, DM
Orekhov, VY
Arseniev, AS
机构
[1] Shemyakin Ovchinnikov Inst. Bioorg., Russian Academy of Sciences, Ul. Miklukho-Maklaya 16/10
基金
俄罗斯基础研究基金会;
关键词
D O I
10.1006/jmre.1997.1190
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Model calculations presented in this article show that commonly used methodology of N-15 relaxation data analysis completely fails in detecting nanosecond time scale motions if the major part of the molecule is involved in these motions. New criteria are introduced for the detection of such cases, based on the dependence of the apparent overall correlation lime, derived from the T-1/T-2 ratio, on the spectrometer frequency. Correctly estimating the overall rotation correlation time tau(R) tvas shown to play the key role in model-free data analysis, It is found, however, that in cases of slow internal motions with characteristic times of more than 3-4 ns, the effective tau(R) provided by the T-1/T-2 ratio for individual amide nitrogens can be used for the characterization of the fast picosecond internal dynamics. (C) 1997 Academic Press.
引用
收藏
页码:184 / 191
页数:8
相关论文
共 31 条
[1]  
ABRAGAM A, 1961, PRINCIPLES NUCLEAR M
[2]  
[Anonymous], 1981, NMR MOL BIOL
[3]   PREDICTING PROTEIN DIFFUSION-COEFFICIENTS [J].
BRUNE, D ;
KIM, S .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1993, 90 (09) :3835-3839
[4]   LONG-RANGE MOTIONAL RESTRICTIONS IN A MULTIDOMAIN ZINC-FINGER PROTEIN FROM ANISOTROPIC TUMBLING [J].
BRUSCHWEILER, R ;
LIAO, XB ;
WRIGHT, PE .
SCIENCE, 1995, 268 (5212) :886-889
[5]   STRUCTURAL DETERMINANTS OF PROTEIN DYNAMICS - ANALYSIS OF N-15 NMR RELAXATION MEASUREMENTS FOR MAIN-CHAIN AND SIDE-CHAIN NUCLEI OF HEN EGG-WHITE LYSOZYME [J].
BUCK, M ;
BOYD, J ;
REDFIELD, C ;
MACKENZIE, DA ;
JEENES, DJ ;
ARCHER, DB ;
DOBSON, CM .
BIOCHEMISTRY, 1995, 34 (12) :4041-4055
[6]   DEVIATIONS FROM THE SIMPLE 2-PARAMETER MODEL-FREE APPROACH TO THE INTERPRETATION OF N-15 NUCLEAR MAGNETIC-RELAXATION OF PROTEINS [J].
CLORE, GM ;
SZABO, A ;
BAX, A ;
KAY, LE ;
DRISCOLL, PC ;
GRONENBORN, AM .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1990, 112 (12) :4989-4991
[7]  
CORDIER F, 1996, NMR, V7, P163
[8]  
DUBIN SB, 1971, J CHEM PHYS, V14, P5138
[9]   DYNAMICS OF THE DIHYDROFOLATE-REDUCTASE FOLATE COMPLEX - CATALYTIC SITES AND REGIONS KNOWN TO UNDERGO CONFORMATIONAL CHANGE EXHIBIT DIVERSE DYNAMICAL FEATURES [J].
EPSTEIN, DM ;
BENKOVIC, SJ ;
WRIGHT, PE .
BIOCHEMISTRY, 1995, 34 (35) :11037-11048
[10]   A COMPARISON OF N-15 NMR RELAXATION MEASUREMENTS WITH A MOLECULAR-DYNAMICS SIMULATION - BACKBONE DYNAMICS OF THE GLUCOCORTICOID RECEPTOR DNA-BINDING DOMAIN [J].
ERIKSSON, MAL ;
BERGLUND, H ;
HARD, T ;
NILSSON, L .
PROTEINS-STRUCTURE FUNCTION AND GENETICS, 1993, 17 (04) :375-390