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

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• 作者：Enrico Rennella ; Thomas Cutuil ; Paul Schanda ; Isabel Ayala ; Vincent Forge ; Bernhard Brutscher
• 刊名：The Journal of the American Chemical Society
• 出版年：2012
• 出版时间：May 16, 2012
• 年：2012
• 卷：134
• 期：19
• 页码：8066-8069
• 全文大小：291K
• 年卷期：v.134,no.19(May 16, 2012)
• ISSN：1520-5126

文摘

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 尾2-microglobulin that has a half-lifetime of only 20 min.