Probing Conformational Exchange Dynamics in a Short-Lived Protein Folding Intermediate by Real-Time Relaxation-Dispersion NMR

J Am Chem Soc. 2017 Jan 25;139(3):1065-1068. doi: 10.1021/jacs.6b12089. Epub 2017 Jan 11.


NMR spectroscopy is a powerful tool for studying molecular dynamics at atomic resolution simultaneously for a large number of nuclear sites. In this communication, we combine two powerful NMR techniques, relaxation-dispersion NMR and real-time NMR, in order to obtain unprecedented information on the conformational exchange dynamics present in short-lived excited protein states, such as those transiently accumulated during protein folding. We demonstrate the feasibility of the approach for the amyloidogenic protein β2-microglobulin that folds via an intermediate state which is believed to be responsible for the onset of the aggregation process leading to amyloid formation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Humans
  • Molecular Dynamics Simulation*
  • Nuclear Magnetic Resonance, Biomolecular*
  • Protein Conformation
  • Protein Folding
  • Time Factors
  • beta 2-Microglobulin / chemistry*


  • beta 2-Microglobulin