Protein dynamics detected by magic-angle spinning relaxation dispersion NMR

Magic-angle spinning (MAS) nuclear magnetic resonance (NMR) is establishing itself as a powerful method for the characterization of protein dynamics at the atomic scale. We discuss here how R1r MAS relaxation dispersion NMR can explore microsecond-to-millisecond motions. Progress in instrumentation, isotope labeling, and pulse sequence design has paved the way for quantitative analyses of even rare structural fluctuations. In addition to isotropic chemical-shift fluctuations exploited in solution-state NMR relaxation disper-sion experiments, MAS NMR has a wider arsenal of observ-ables, allowing to see motions even if the exchanging states do not differ in their chemical shifts. We demonstrate the potential of the technique for probing motions in challenging large en-zymes, membrane proteins, and protein assemblies.

Automated summary

Magic-angle spinning (MAS) nuclear magnetic resonance (NMR) is a powerful method for characterizing protein dynamics at the atomic scale. The R1r MAS relaxation dispersion NMR technique allows exploration of microsecond-to-millisecond motions. This technique has the potential to probe motions in challenging systems such as large enzymes, membrane proteins, and protein assemblies.