核磁共振探测与可视化内在无序蛋白质中的相关结构波动

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

作者信息

Kurzbach Dennis, Beier Andreas, Vanas Agathe, Flamm Andrea G, Platzer Gerald, Schwarz Thomas C, Konrat Robert

机构信息

Département de Chimie, Ecole Normale Supérieure, PSL Research University, UPMC Univ Paris 06, CNRS, Laboratoire des Biomolécules (LBM), 24 rue Lhomond, 75005 Paris, France.

出版信息

Phys Chem Chem Phys. 2017 Apr 19;19(16):10651-10656. doi: 10.1039/c7cp00430c.

DOI:10.1039/c7cp00430c

PMID:28397898

Abstract

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.

摘要

基于相关矩阵的计算，提出了一种对基于顺磁弛豫增强（PRE）和顺磁弛豫干扰（PRI）的核磁共振（NMR）数据进行新颖统计分析的方法。以内在无序蛋白（IDP）骨桥蛋白（OPN）和脑酸溶性蛋白1（BASP1）为例对该技术进行了演示。相关性分析详细地可视化了IDP中构象平均的微妙之处，并突出了IDP中各个子域相关结构波动的存在。