Issue 16, 2017
From the journal:

Physical Chemistry Chemical Physics

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

Dennis Kurzbach, ORCID logo *ab   Andreas Beier,c   Agathe Vanas,c   Andrea G. Flamm,c   Gerald Platzer,c   Thomas C. Schwarzc  and  Robert Konrat*c  

* Corresponding authors

a Département de Chimie, Ecole Normale Supérieure, PSL Research University, UPMC Univ Paris 06, CNRS, Laboratoire des Biomolécules (LBM), 24 rue Lhomond, 75005 Paris, France
E-mail: kurzbach@ens.fr

b Sorbonne Universités, UPMC Univ Paris 06, Ecole Normale Supérieure, CNRS, Laboratoire des Biomolecules (LBM), Paris, France

c Department for Structural and Computational Biology, Max F. Perutz Laboratories, University of Vienna, Vienna Biocenter Campus 5, 1030 Vienna, Austria
E-mail: robert.konrat@univie.ac.at

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.

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

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Article information

DOI
https://doi.org/10.1039/C7CP00430C
Article type
Paper
Submitted
19 Jan 2017
Accepted
27 Mar 2017
First published
28 Mar 2017

Phys. Chem. Chem. Phys., 2017,19, 10651-10656

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

D. Kurzbach, A. Beier, A. Vanas, A. G. Flamm, G. Platzer, T. C. Schwarz and R. Konrat, Phys. Chem. Chem. Phys., 2017, 19, 10651 DOI: 10.1039/C7CP00430C

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