Molecular dynamics and NMR spin relaxation in proteins

Acc Chem Res. 2002 Jun;35(6):325-31. doi: 10.1021/ar010020l.

Abstract

Molecular dynamics simulations often play a central role in the analysis of biomolecular NMR data. The focus here is on NMR spin-relaxation, which can provide unique insights into the time-dependence of conformational fluctuations, especially on picosecond to nanosecond time scales which can be directly probed by simulations. A great deal has been learned from such simulations about the general nature of such motions and their impact on NMR observables. In principle, relaxation measurements should also provide valuable benchmarks for judging the quantitative accuracy of simulations, but there are a variety of experimental and computational obstacles to making useful direct comparisons. It seems likely that simulations on time scales that are just now becoming generally feasible may provide important new information on internal motions, overall rotational diffusion, and the coupling between internal and rotational motion. Such information could provide a sound foundation for a new generation of detailed interpretation of NMR spin-relaxation results.

Publication types

  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Computer Simulation
  • Diffusion
  • Models, Molecular*
  • Motion
  • Nuclear Magnetic Resonance, Biomolecular*
  • Proteins / chemistry*

Substances

  • Proteins