High-resolution characterization of intrinsic disorder in proteins: expanding the suite of (13)C-detected NMR spectroscopy experiments to determine key observables

Chembiochem. 2011 Oct 17;12(15):2347-52. doi: 10.1002/cbic.201100406.

Abstract

Order in disorder: The characterization of intrinsically disordered proteins by NMR spectroscopy is a necessity on the one hand and a continuous challenge on the other. We propose two experiments that provide diagnostic parameters to monitor the degree of unfolding of a polypeptide. The test was performed on the yeast Cox17 protein, known to gain its function through maturation from an intrinsically disordered state (see figure).

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cation Transport Proteins / chemistry*
  • Copper Transport Proteins
  • Disulfides / chemistry
  • Models, Molecular
  • Molecular Chaperones / chemistry*
  • Nuclear Magnetic Resonance, Biomolecular*
  • Oxidation-Reduction
  • Protein Conformation
  • Protein Unfolding*
  • Saccharomyces cerevisiae / chemistry*
  • Saccharomyces cerevisiae Proteins / chemistry*

Substances

  • COX17 protein, S cerevisiae
  • Cation Transport Proteins
  • Copper Transport Proteins
  • Disulfides
  • Molecular Chaperones
  • Saccharomyces cerevisiae Proteins