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

Phys Chem Chem Phys

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

Published: April 2017

AI Article Synopsis

  • A new statistical method is introduced for analyzing paramagnetic relaxation enhancement (PRE) and paramagnetic relaxation interference (PRI) data using correlation matrices in nuclear magnetic resonance (NMR) studies.
  • The technique is illustrated with the proteins osteopontin (OPN) and brain acid soluble protein 1 (BASP1), both of which are intrinsically disordered proteins (IDPs).
  • This correlation analysis reveals detailed insights into how IDPs undergo conformational averaging and demonstrates the correlated structural fluctuations within their individual sub-domains.

Article 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.

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http://dx.doi.org/10.1039/c7cp00430cDOI Listing

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