COMPARISON OF THE C-13 RELAXATION-TIMES AND PROTON SCALAR COUPLINGS OF BPTI WITH VALUES PREDICTED BY MOLECULAR-DYNAMICS

被引：16

作者：

BALASUBRAMANIAN, S ^{[1
]}

NIRMALA, R ^{[1
]}

BEVERIDGE, DL ^{[1
]}

BOLTON, PH ^{[1
]}

机构：

[1] WESLEYAN UNIV,DEPT CHEM,MIDDLETOWN,CT 06459

来源：

JOURNAL OF MAGNETIC RESONANCE SERIES B | 1994年 / 104卷 / 03期

关键词：

D O I：

10.1006/jmrb.1994.1081

中图分类号：

O64 [物理化学（理论化学）、化学物理学]; O56 [分子物理学、原子物理学];

学科分类号：

070203 ; 070304 ; 081704 ; 1406 ;

摘要：

The experimental carbon-13 relaxation times of BPTI have been compared with the values predicted by molecular-dynamics simulations. Since the carbon-13 T-1 values are sensitive monitors of the rates and amplitudes of the internal motions of the protein, this comparison was made to test the extent to which molecular dynamics provides an accurate depiction of the internal motions of proteins. The experimental and predicted amide-alpha scalar couplings were also compared, since this coupling is dependent on the conformation of the protein. These comparisons have shown that the molecular-dynamics simulation predicts results that are in good overall agreement with the experimental data. (C) 1994 Academic Press, Inc.

引用

页码：240 / 249

页数：10

共 37 条

[1] BACKBONE DYNAMICS OF CALMODULIN STUDIED BY N-15 RELAXATION USING INVERSE DETECTED 2-DIMENSIONAL NMR-SPECTROSCOPY - THE CENTRAL HELIX IS FLEXIBLE [J].