Local structure and anisotropic backbone dynamics from cross-correlated NMR relaxation in proteins

被引：9
|
作者：
Markwick, PRL [1 ]
Sprangers, R [1 ]
Sattler, M [1 ]
机构：
[1] European Mol Biol Lab, D-69117 Heidelberg, Germany
来源：
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2005年 / 44卷 / 21期
关键词：
chemical shift anisotropy; density functional calculations; molecular dynamics; NMR spectroscopy; structure elucidation;
D O I：
10.1002/anie.200462495
中图分类号：
O6 [化学];
学科分类号：
0703 ;
摘要：
Cross-correlated relaxation (CCR) can be used to describe the structure and dynamics of biomolecules (see picture). By combining theoretical and experimental techniques in the study of proteins, for example, it is possible to acquire detailed information concerning the local anisotropic motion of the peptide plane (Chemical Equation Presented) from a single cross-correlation: the C′/N-H CCR rate. © 2005 Wiley-VCH Verlag GmbH & Co. KGaA.
引用
收藏
页码：3232 / 3237
页数：6
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