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Article Dans Une Revue Journal of the American Chemical Society Année : 2012

Real-Time NMR Characterization of Structure and Dynamics in a Transiently Populated Protein Folding Intermediate

Résumé

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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Dates et versions

hal-01130171 , version 1 (11-03-2015)

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Enrico Rennella, Thomas Cutuil, Paul Schanda, Isabel Ayala, Vincent Forge, et al.. Real-Time NMR Characterization of Structure and Dynamics in a Transiently Populated Protein Folding Intermediate. Journal of the American Chemical Society, 2012, 134 (19), pp.8066-8069. ⟨10.1021/ja302598j⟩. ⟨hal-01130171⟩
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