Vögeli, B. et al. Nat. Struct. Mol. Biol. 19, 1053–1057 (2012).

Proteins are not static entities; rather, their structures constantly fluctuate between different conformational states. Detecting and understanding this dynamic motion is crucial to understanding how proteins function. Although nuclear magnetic resonance (NMR) spectroscopy has provided valuable insights into local molecular dynamics, no method so far has been able to detect concerted motion or motion through space. Vögeli et al. now show that it is possible to use exact nuclear Overhauser enhancement (NOE) rates to determine ensemble-averaged distance restraints. NOE measurements, which reflect through-space spin-spin coupling between NMR-active nuclei, are commonly applied in NMR-based three-dimensional structure determination of proteins. Vögeli et al. now apply their method for calculating exact NOE rates for ensemble-based structure determination to the model protein GB3, obtaining both its structure and a description of its dynamics.