Determining domain orientation in macromolecules by using spin-relaxation and residual dipolar coupling measurements

被引：80

作者：

Fushman, D ^{[1
]}

Varadan, R ^{[1
]}

Assfalg, M ^{[1
]}

Walker, O ^{[1
]}

机构：

[1] Univ Maryland, Ctr Biomol Struct & Org, Dept Chem & Biochem, College Pk, MD 20742 USA

来源：

PROGRESS IN NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY | 2004年 / 44卷 / 3-4期

基金：

美国国家卫生研究院;

关键词：

domain orientation; residual dipolar couplings; rotational diffusion; interdomain dynamics; spin relaxation; spin labeling; ubiquitin; polyubiquitin;

D O I：

10.1016/j.pnmrs.2004.02.001

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

The structural characterization of multidomain protein complexes was studied using spin-relaxation and dipolar coupling measurements. The internuclear anisotropy of molecular tumbling was determined by NMR approaches. It was found that the interdomain interface was formed by hydrophobic patches. The interdomain dynamics allowed the L8, 144, and V70 groups to interact with other molecules. The features of anisotropic tumbling and tensor determination were explored by using computer-generated relaxation data.

引用

页码：189 / 214

页数：26

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