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Your search keyword '"EU IRG (PIRG03-GA-2008-231026)."' showing total 3 results
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3 results on '"EU IRG (PIRG03-GA-2008-231026)."'

1. Site-Specific Measurement of Slow Motions in Proteins

Author

Lyndon Emsley, Martin Blackledge, Stephan Grzesiek, Hans Juergen Sass, Józef R. Lewandowski, ISA - Centre de RMN à très hauts champs, Institut des Sciences Analytiques (ISA), 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), Biozentrum [Basel, Suisse], University of Basel (Unibas), 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), Agence Nationale de la Recherche (ANR PCV 2007 Protein Motion), EU PIRG03-GA-2008-231026, Seventh Framework Program of the EC (BioNMR 261863), EU IRG (PIRG03-GA-2008-231026), Swiss National Science Foundation (grant 31-132857)., European Project, 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), 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, 010405 organic chemistry, Chemistry, Analytical chemistry, Proteins, General Chemistry, 010402 general chemistry, 01 natural sciences, Biochemistry, Catalysis, 0104 chemical sciences, Quantitative measure, Motion, Colloid and Surface Chemistry, [CHIM.ANAL]Chemical Sciences/Analytical chemistry, Chemical physics, Molecular motion, Relaxation (physics)
Abstract

International audience; We demonstrate that a quantitative measure of slow molecular motions in solid proteins can be accessed by measuring site-specific (15)N rotating-frame relaxation rates at high magic-angle-spinning frequencies.

Published
2011
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2. Enhanced resolution and coherence lifetimes in the solid-state NMR spectroscopy of perdeuterated proteins under ultrafast magic-angle spinning

Author

Lyndon Emsley, Józef R. Lewandowski, Sascha Lange, Hartmut Oschkinat, Uemit Akbey, Jean-Nicolas Dumez, 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), Leibniz Forschungsinstitut für Molekulare Pharmakolgie = Leibniz Institute for Molecular Pharmacology [Berlin, Allemagne] (FMP), Leibniz Association, Agence Nationale de la Recherche (ANR PCV 2007 Protein Motion), DFG (SFB 740), Access to Research Infrastructures activity in the seventh Framework Program of the EC (BioNMR 261863), EU IRG (PIRG03-GA-2008-231026)., 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), and Université de Lyon-Université de Lyon-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)

Subjects
Analytical chemistry, ASSIGNMENT, Field strength, 010402 general chemistry, 01 natural sciences, LATTICE-RELAXATION, [CHIM.ANAL]Chemical Sciences/Analytical chemistry, Magic angle spinning, General Materials Science, RATES, Physical and Theoretical Chemistry, Spectroscopy, Spinning, 010405 organic chemistry, Chemistry, H-1, CRYSTALLINE PROTEIN, DEUTERATION, QUANTITATIVE-ANALYSIS, 0104 chemical sciences, NMR spectra database, [CHIM.THEO]Chemical Sciences/Theoretical and/or physical chemistry, Microcrystalline, Solid-state nuclear magnetic resonance, ROTATING SOLIDS, BACKBONE DYNAMICS, [PHYS.PHYS.PHYS-CHEM-PH]Physics [physics]/Physics [physics]/Chemical Physics [physics.chem-ph], SENSITIVITY, Coherence (physics)
Abstract

International audience; We investigate the combined effect of perdeuteration and fast magic-angle spinning on the resolution and sensitivity of proton-detected protein NMR spectra and on coherence lifetimes. With 60 kHz spinning of a microcrystalline alpha-spectrin SH3 sample at a field strength of 23 T, a regime is attained where there is no substantial difference in resolution between perdeuterated samples with 10 or 100% protons at the exchangeable sites. (1)H resolution is then limited by inhomogeneous contributions. Upon fast spinning, the most dramatic line narrowing effects are observed for residues in the loop or bend regions of the protein, probably due to the removal of destructive dynamics effects. This investigation paves the way for using samples with 100% protons at the exchangeable sites in structure determination protocols, since all backbone amide sites can now contribute to the signal.

Published
2011
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3. High-resolution and sensitivity through-bond correlations in ultra-fast magic angle spinning (MAS) solid-state NMR

Author

Lyndon Emsley, Ivano Bertini, Józef R. Lewandowski, Ségolène Laage, Isabella C. Felli, Anne Lesage, Guido Pintacuda, Roberta Pierattelli, Alessandro Marchetti, Dept Chem Ugo Schiff, Università degli Studi di Firenze = University of Florence [Firenze] (UNIFI), Magnet Resonance Ctr CERM, 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), Scuola Normale Superiore di Pisa (SNS), Agence Nationale de la Recherche (ANR 08-BLAN-0035-01), Ente Cassa di Risparmio di Firenze, from Egide (programme Galilee 22397RJ), the Universita Italo-Francese (Programma Galileo 2009/2010), Joint Research Activity and Access to Research Infrastructures activity in the 6th Framework Program of the EC (RII3-026145, EU-NMR), EU IRG (PIRG03-GA-2008-231026)., European Project, Università degli Studi di Firenze = University of Florence (UniFI), 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), and Université de Lyon-Université de Lyon-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)

Subjects
SELECTION, Spin states, PROTEINS, C-13, Analytical chemistry, 010402 general chemistry, 01 natural sciences, Homonuclear molecule, ASSIGNMENT STRATEGIES, ENHANCEMENT, [CHIM.ANAL]Chemical Sciences/Analytical chemistry, DISORDERED SOLIDS, Magic angle spinning, Molecule, HETERONUCLEAR CORRELATION, Spectroscopy, HOMONUCLEAR, chemistry.chemical_classification, SPECTROSCOPY, 010405 organic chemistry, Biomolecule, General Chemistry, 0104 chemical sciences, Microcrystalline, Solid-state nuclear magnetic resonance, chemistry, Chemical physics, CROSS-POLARIZATION
Abstract

International audience; We introduce a new experiment, which makes use of Spin State Selective manipulations to perform sensitive and resolved through-bond correlations in organic and biological solids at high-fields and under ultra-fast MAS. The scheme is the shortest and most sensitive through-bond correlation method introduced so far in solids, yields resolved fingerprints of uniformly (13)C-labeled biomolecules, and constitutes a tool to highlight slight static structural disorder around crystallographically equivalent molecules in microcrystalline samples.

Published
2011
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