An NMR method to study protein-protein interactions

Methods Mol Biol. 2012;757:129-37. doi: 10.1007/978-1-61779-166-6_10.

Abstract

Specific interactions between proteins are a fundamental process underlying the various biological events, such as cell-cell contacts, signal transduction, and gene expression. Therefore, the structural investigations of protein-protein interactions provide useful information for understanding these events. We describe an NMR method, termed the cross-saturation (CS) method, to determine the binding sites of protein complexes more precisely than conventional NMR methods. The CS method can determine the binding sites of a protein complex that undergoes fast exchange between the free and the bound states, regardless of the molecular size of the complex.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Models, Molecular
  • Nuclear Magnetic Resonance, Biomolecular*
  • Protein Binding
  • Protein Denaturation
  • Protein Interaction Mapping*
  • Protein Structure, Tertiary
  • Proteins / chemistry*
  • Proteins / metabolism*

Substances

  • Proteins