NMR contributions to structural dynamics studies of intrinsically disordered proteins

被引：136

作者：

Konrat, Robert ^{[1
]}

机构：

[1] Univ Vienna, Max F Perutz Labs, Dept Struct & Computat Biol, A-1030 Vienna, Austria

来源：

JOURNAL OF MAGNETIC RESONANCE | 2014年 / 241卷

基金：

奥地利科学基金会;

关键词：

Intrinsically disordered proteins; Protein meta-structure; Structural biology; Biomolecular NMR; EPR spectroscopy; NMR spin relaxation; RESIDUAL DIPOLAR COUPLINGS; NUCLEAR-MAGNETIC-RESONANCE; CHEMICAL-SHIFTS; UNFOLDED PROTEINS; RELAXATION; DOMAIN; STATES; ENSEMBLES; PROPENSITIES; BIOMOLECULES;

D O I：

10.1016/j.jmr.2013.11.011

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Intrinsically disordered proteins (IDPs) are characterized by substantial conformational plasticity. Given their inherent structural flexibility X-ray crystallography is not applicable to study these proteins. In contrast, NMR spectroscopy offers unique opportunities for structural and dynamic studies of IDPs. The past two decades have witnessed significant development of NMR spectroscopy that couples advances in spin physics and chemistry with a broad range of applications. This article will summarize key advances in basic physical-chemistry and NMR methodology, outline their limitations and envision future R&D directions. (c) 2013 The Author. Published by Elsevier Inc. All rights reserved.

引用

页码：74 / 85

页数：12

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