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Updated: May 22, 2026

NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins
Published on: November 1, 2024
Real-time NMR characterization of structure and dynamics in a transiently populated protein folding intermediate
Enrico Rennella1, Thomas Cutuil, Paul Schanda
1Institut de Biologie Structurale, Université Grenoble 1, CEA, CNRS, 41 rue Jules Horowitz, 38027 Grenoble Cedex 1, France.
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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