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

Abstract : 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.
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Article dans une revue
Journal of the American Chemical Society, American Chemical Society, 2017, 139 (3), pp.1065-1068. 〈10.1021/jacs.6b12089〉
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Soumis le : lundi 13 février 2017 - 09:06:44
Dernière modification le : lundi 19 février 2018 - 14:34:04

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Rémi Franco, Sergio Gil-Caballero, Isabel Ayala, Adrien Favier, Bernhard Brutscher. Probing Conformational Exchange Dynamics in a Short-Lived Protein Folding Intermediate by Real-Time Relaxation-Dispersion NMR.. Journal of the American Chemical Society, American Chemical Society, 2017, 139 (3), pp.1065-1068. 〈10.1021/jacs.6b12089〉. 〈hal-01465682〉

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