Simultaneous determination of fast and slow dynamics in molecules using extreme CPMG relaxation dispersion experiments

J Biomol NMR. 2018 Jan;70(1):1-9. doi: 10.1007/s10858-017-0155-0. Epub 2017 Nov 29.

Abstract

Molecular dynamics play a significant role in how molecules perform their function. A critical method that provides information on dynamics, at the atomic level, is NMR-based relaxation dispersion (RD) experiments. RD experiments have been utilized for understanding multiple biological processes occurring at micro-to-millisecond time, such as enzyme catalysis, molecular recognition, ligand binding and protein folding. Here, we applied the recently developed high-power RD concept to the Carr-Purcell-Meiboom-Gill sequence (extreme CPMG; E-CPMG) for the simultaneous detection of fast and slow dynamics. Using a fast folding protein, gpW, we have shown that previously inaccessible kinetics can be accessed with the improved precision and efficiency of the measurement by using this experiment.

Keywords: Conformational exchange; Extreme CPMG; Protein dynamics; Relaxation dispersion; µs–ms dynamics.

MeSH terms

  • Kinetics
  • Models, Molecular*
  • Molecular Dynamics Simulation*
  • Nuclear Magnetic Resonance, Biomolecular / methods*
  • Protein Conformation
  • Protein Folding
  • Viral Structural Proteins / chemistry

Substances

  • Viral Structural Proteins
  • protein W, bacteriophage lambda