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

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• 作者：Rémi Franco ; Sergio Gil-Caballero ; Isabel Ayala ; Adrien Favier ; Bernhard Brutscher
• 刊名：Journal of the American Chemical Society
• 出版年：2017
• 出版时间：January 25, 2017
• 年：2017
• 卷：139
• 期：3
• 页码：1065-1068
• 全文大小：311K
• ISSN：1520-5126

文摘

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.