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

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

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

Phys Chem Chem Phys. 2017 Apr 11;:

Authors: Kurzbach D, Beier A, Vanas A, Flamm AG, Platzer G, Schwarz TC, Konrat R

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.


PMID: 28397898 [PubMed - as supplied by publisher]



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