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

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

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Edité par CCSD ; American Chemical Society -

International audience. 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.

Langue: en

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