Real-time NMR characterization of structure and dynamics in a transiently populated protein folding intermediate

Journal of the American Chemical Society
Enrico RennellaBernhard Brutscher

Abstract

Recent advances in NMR spectroscopy and the availability of high magnetic field strengths now offer the possibility to record real-time 3D NMR spectra of short-lived protein states, e.g., states that become transiently populated during protein folding. Here we present a strategy for obtaining sequential NMR assignments as well as atom-resolved information on structural and dynamic features within a folding intermediate of the amyloidogenic protein β2-microglobulin that has a half-lifetime of only 20 min.

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Citations

Jan 18, 2014·Journal of Biomolecular NMR·Maxim MayzelVladislav Y Orekhov
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