Distance-independent Cross-correlated Relaxation and Isotropic Chemical Shift Modulation in Protein Dynamics Studies

Chemphyschem. 2019 Jan 21;20(2):178-196. doi: 10.1002/cphc.201800602. Epub 2018 Sep 3.

Abstract

Cross-correlated relaxation (CCR) in multiple-quantum coherences differs from other relaxation phenomena in its theoretical ability to be mediated across an infinite distance. The two interfering relaxation mechanisms may be dipolar interactions, chemical shift anisotropies, chemical shift modulations or quadrupolar interactions. These properties make multiple-quantum CCR an attractive probe for structure and dynamics of biomacromolecules not accessible from other measurements. Here, we review the use of multiple-quantum CCR measurements in dynamics studies of proteins. We compile a list of all experiments proposed for CCR rate measurements, provide an overview of the theory with a focus on protein dynamics, and present applications to various protein systems.

Keywords: biomacromolecules; correlated motion; cross-correlated relaxation; multiple-quantum coherence; protein dynamics.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Models, Theoretical
  • Nuclear Magnetic Resonance, Biomolecular
  • Protein Conformation
  • Proteins / chemistry*
  • Proteins / metabolism
  • Quantum Theory

Substances

  • Proteins