4.6 Article

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

Journal

PHYSICAL CHEMISTRY CHEMICAL PHYSICS
Volume 19, Issue 16, Pages 10651-10656

Publisher

ROYAL SOC CHEMISTRY
DOI: 10.1039/c7cp00430c

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Funding

  1. Humboldt Foundation
  2. Austrian Science Foundation (FWF) [P26317, I844]
  3. Austrian Science Fund (FWF) [I844, P26317] Funding Source: Austrian Science Fund (FWF)

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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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