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

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

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.

MeSH terms

  • Humans
  • Intrinsically Disordered Proteins / chemistry*
  • Intrinsically Disordered Proteins / metabolism
  • Membrane Proteins / chemistry
  • Membrane Proteins / metabolism
  • Models, Molecular
  • Nerve Tissue Proteins / chemistry
  • Nerve Tissue Proteins / metabolism
  • Nuclear Magnetic Resonance, Biomolecular*
  • Osteopontin / chemistry
  • Osteopontin / metabolism
  • Protein Structure, Tertiary
  • Repressor Proteins / chemistry
  • Repressor Proteins / metabolism

Substances

  • BASP1 protein, human
  • Intrinsically Disordered Proteins
  • Membrane Proteins
  • Nerve Tissue Proteins
  • Repressor Proteins
  • Osteopontin