title: Real-time NMR characterization of structure and dynamics in a transiently populated protein folding intermediate.
abstract: 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.
authors.affiliation: Institut de Biologie Structurale, Université Grenoble 1, CEA, CNRS, 41 rue Jules Horowitz, 38027 Grenoble Cedex 1, France.
authors.forename: Enrico
authors.initials: E
authors.lastname: Rennella
authors.forename: Thomas
authors.initials: T
authors.lastname: Cutuil
authors.forename: Paul
authors.initials: P
authors.lastname: Schanda
authors.forename: Isabel
authors.initials: I
authors.lastname: Ayala
authors.forename: Vincent
authors.initials: V
authors.lastname: Forge
authors.forename: Bernhard
authors.initials: B
authors.lastname: Brutscher
mesh_terms: D006801:Humans; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008958:Models, Molecular; D017510:Protein Folding; D017433:Protein Structure, Secondary; D013997:Time Factors; D001613:beta 2-Microglobulin / Q000737:chemistry*
chemical_list: D001613:beta 2-Microglobulin