1. Real-Time NMR Characterization of Structure and Dynamics in a Transiently Populated Protein Folding Intermediate
- Author
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Thomas Cutuil, Bernhard Brutscher, Vincent Forge, Enrico Rennella, Isabel Ayala, Paul Schanda, Institut de biologie structurale (IBS - UMR 5075 ), Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Laboratoire de Chimie et Biologie des Métaux (LCBM - UMR 5249), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), and Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)
- Subjects
Models, Molecular ,Protein Folding ,Magnetic Resonance Spectroscopy ,Time Factors ,MULTIDIMENSIONAL NMR ,REFOLDING INTERMEDIATE ,010402 general chemistry ,01 natural sciences ,Biochemistry ,Protein Structure, Secondary ,Catalysis ,03 medical and health sciences ,Colloid and Surface Chemistry ,Protein structure ,BETA(2)-MICROGLOBULIN ,ATOMIC-RESOLUTION ,[CHIM]Chemical Sciences ,Humans ,[SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology ,Spectroscopy ,030304 developmental biology ,0303 health sciences ,SPECTROSCOPY ,Chemistry ,General Chemistry ,Nuclear magnetic resonance spectroscopy ,0104 chemical sciences ,Characterization (materials science) ,Folding (chemistry) ,NMR spectra database ,Crystallography ,AMYLOID FORMATION ,Protein folding ,beta 2-Microglobulin ,High magnetic field - Abstract
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.
- Published
- 2012
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