NMR probing and visualization of correlated structural fluctuations in intrinsically disordered proteins

被引：17

作者：

Kurzbach, Dennis ^{[1
,2
]}

Beier, Andreas ^{[3
]}

Vanas, Agathe ^{[3
]}

Flamm, Andrea G. ^{[3
]}

Platzer, Gerald ^{[3
]}

Schwarz, Thomas C. ^{[3
]}

Konrat, Robert ^{[3
]}

机构：

[1] UPMC Univ Paris 06, PSL Res Univ, Ecole Normale Super, Dept Chim,LBM,CNRS, 24 Rue Lhomond, F-75005 Paris, France

[2] UPMC Univ Paris 06, Sorbonne Univ, Ecole Normale Super, CNRS,LBM, Paris, France

[3] Univ Vienna, Max F Perutz Labs, Dept Struct & Computat Biol, Vienna Bioctr Campus 5, A-1030 Vienna, Austria

来源：

PHYSICAL CHEMISTRY CHEMICAL PHYSICS | 2017年 / 19卷 / 16期

基金：

奥地利科学基金会;

关键词：

PROTON RELAXATION-TIMES; NETWORK REPRESENTATION; PARAMAGNETIC SOLUTIONS; UNSTRUCTURED PROTEINS; OSTEOPONTIN; DYNAMICS; RECOGNITION;

D O I：

10.1039/c7cp00430c

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：

A novel statistical analysis of paramagnetic relaxation enhancement (PRE) and paramagnetic relaxation interference (PRI) based nuclear magnetic resonance (NMR) data is proposed based on the computation of correlation matrices. The technique is demonstrated with an example of the intrinsically disordered proteins (IDPs) osteopontin (OPN) and brain acid soluble protein 1 (BASP1). The correlation analysis visualizes in detail the subtleties of conformational averaging in IDPs and highlights the presence of correlated structural fluctuations of individual sub- domains in IDPs.

引用

页码：10651 / 10656

页数：6

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