Fast resonance assignment and fold determination of human superoxide dismutase by high-resolution proton-detected solid-state MAS NMR spectroscopy
| Autor: | Andrew J. Pell, Anne Lesage, Ivano Bertini, Torsten Herrmann, Lyndon Emsley, Guido Pintacuda, Amy L. Webber, Paul Guerry, Leonardo Gonnelli, Emeline Barbet-Massin, Michael J. Knight, Roberta Pierattelli, Isabella C. Felli |
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| Přispěvatelé: | ISA - Centre de RMN à très hauts champs, Institut des Sciences Analytiques (ISA), Institut de Chimie du CNRS (INC)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS), Dept Chem Ugo Schiff, Università degli Studi di Firenze = University of Florence [Firenze] (UNIFI), Magnet Resonance Ctr CERM, Magnetic Resonance Center, Agence Nationale de la Recherche (ANR 08-BLAN-0035-01 and 10-BLAN-713-01), Ente Cassa di Risparmio di Firenze, Egide (programme Galiee 22397RJ), the Universita Italo-francese (programma Galileo 09/10), Joint Research Activity and Access to Research Infrastructures in the 7th Framework program of the EC (BioNMR n. 261863)., European Project, Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Università degli Studi di Firenze = University of Florence (UniFI) |
| Rok vydání: | 2011 |
| Předmět: |
Models
Molecular Protein Folding C-13 Protein Conformation Analytical chemistry Solid-state 010402 general chemistry 01 natural sciences Catalysis Spectral line 3D STRUCTURE DETERMINATION Superoxide dismutase Protein structure NMR spectroscopy RESTRAINTS [CHIM.ANAL]Chemical Sciences/Analytical chemistry LARGER PROTEINS structural constraints COHERENCE SPECTRA Humans protein structure WILD-TYPE Nuclear Magnetic Resonance Biomolecular ComputingMilieux_MISCELLANEOUS 1H detection Mas nmr spectroscopy biology Chemistry 010405 organic chemistry MEMBRANE-PROTEINS Superoxide Dismutase General Chemistry Nuclear magnetic resonance spectroscopy General Medicine 0104 chemical sciences NMR spectra database Microcrystalline PROTEIN-STRUCTURE DETERMINATION biology.protein PERDEUTERATED PROTEINS Protons |
| Zdroj: | Angewandte Chemie International Edition Angewandte Chemie International Edition, Wiley-VCH Verlag, 2011, 50 (49), pp.11697-11701. ⟨10.1002/anie.201106340⟩ Angewandte Chemie International Edition, 2011, 50 (49), pp.11697-11701. ⟨10.1002/anie.201106340⟩ |
| ISSN: | 1521-3773 1433-7851 |
| Popis: | Re-protonation is key: A combination of a high magnetic field (1 GHz) and ultra-fast magic-angle spinning (60 kHz) allows easy detection of NMR spectra revealing details of secondary and tertiary structures of medium-sized proteins. The technique was applied to the 153-residue microcrystalline Zn II-loaded superoxide dismutase (ZnII-SOD) fully [ 2H,13C,15N]-labeled and 100% re-protonated at the exchangeable sites. Copyright © 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim. |
| Databáze: | OpenAIRE |
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