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Your search keyword '"European Project: 661175,H2020,H2020-MSCA-IF-2014,virus-DNP-NMR(2015)"' showing total 2 results
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2 results on '"European Project: 661175,H2020,H2020-MSCA-IF-2014,virus-DNP-NMR(2015)"'

1. Backbone and side-chain proton NMR assignment in fully protonated proteins: microcrystals, sedimented assemblies, and amyloid fibrils

Author

Stanek, Jan, Andreas, Loren, Jaudzems, Kristaps, Cala, Diane, Lalli, Daniela, Bertarello, Andrea, Schubeis, Tobias, Akopjana, Inara, Kotelovica, Svetlana, Tars, Kaspars, Pica, Andrea, Leone, Serena, Picone, Delia, Xu, Zhi-Qiang, Dixon, Nicholas, Martinez, Denis, Berbon, Melanie, El Mammeri, Nadia, Noubhani, Abdelmajid, Saupe, Sven, Habenstein, Birgit, Loquet, Antoine, Pintacuda, Guido, Biological Solid-State NMR Methods - Méthodes de RMN à l'état solide en biologie, 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), Biomed Res & Study Ctr, Latvian Biomed Res & Study Ctr, Dept Mol Biol, University of Latvia (LU), Dipartimento di Scienze Chimiche, University of Naples Federico II = Università degli studi di Napoli Federico II, School of Chemistry [Wollongong], University of Wollongong [Australia], Chimie et Biologie des Membranes et des Nanoobjets (CBMN), Université de Bordeaux (UB)-École Nationale d'Ingénieurs des Travaux Agricoles - Bordeaux (ENITAB)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Institut de biochimie et génétique cellulaires (IBGC), Université Bordeaux Segalen - Bordeaux 2-Centre National de la Recherche Scientifique (CNRS), Fondation pour la Chimie des Substances Naturelles, IR-RMN FR3050, Fondazione con il Sud (grant 2011- PDR-19), European Project: 648974,H2020,ERC-2014-CoG,P-MEM-NMR(2015), European Project: 639020,H2020,ERC-2014-STG,Weakinteract(2015), European Project: 624918,EC:FP7:PEOPLE,FP7-PEOPLE-2013-IIF,MEM-MAS(2014), European Project: 661799,H2020,H2020-MSCA-IF-2014,COMPLEX-fastMAS-NMR(2016), European Project: 661175,H2020,H2020-MSCA-IF-2014,virus-DNP-NMR(2015), European Project: 317127,EC:FP7:PEOPLE,FP7-PEOPLE-2012-ITN,PNMR(2013), 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), and Università degli studi di Napoli Federico II

Subjects
[CHIM.THEO]Chemical Sciences/Theoretical and/or physical chemistry, magic-angle spinning, proton detection, solid-state NMR spectroscopy, resonance assignment
Abstract

International audience; Wir beschreiben die sensitive Messung von alpha-Protonen in voll protonierten Proteinen durch Festkörper-NMR mit Rotation um den magischen Winkel (MAS) von 100-111 kHz. Die exzellente Auflösung in der Cα-Hα-Ebene wird für 5 Proteine gezeigt, darunter Mikrokristalle, ein sedimentierter Komplex, ein Kapsid und Amyloidfibrillen. Ausgehend davon wurde ein Satz 3D-Spektren für die sequenzspezifische Zuordnung der Rückgrat- und der aliphatischen Seitenketten-Resonanzen entwickelt. Dabei wurden nur 500 μg Probe verwendet. Diese Entwicklungen beschleunigen strukturelle Untersuchungen von biomolekularen Komplexen, die nur in Submilligramm-Mengen verfügbar sind, ohne die Notwendigkeit einer Deuterierung.; We demonstrate sensitive detection of alpha protons of fully protonated proteins by solid-state NMR with 100-111 kHz magic-angle spinning (MAS). The excellent resolution in the Cα-Hα plane is demonstrated for 5 proteins, including microcrystals, a sedimented complex, a capsid and amyloid fibrils. A set of 3D spectra based on a Cα-Hα detection block was developed and applied for the sequence-specific backbone and aliphatic side-chain resonance assignment using only 500 μg of sample. These developments accelerate structural studies of biomolecular assemblies available in submilligram quantities without the need of protein deuteration.

Published
2016
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2. Is protein deuteration beneficial for proton detected solid-state NMR at and above 100 kHz magic-angle spinning?

Author

Kristaps Jaudzems, Guido Pintacuda, Loren B. Andreas, Kaspars Tars, Diane Cala de Paepe, Jan Stanek, Biological Solid-State NMR Methods - Méthodes de RMN à l'état solide en biologie, 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), Biomed Res & Study Ctr, Max Planck Institute for Biophysical Chemistry (MPI-BPC), Max-Planck-Gesellschaft, The financial support from CNRS (IR-RMN FR3050 and Fondation pour la Chimie des Substances Naturelles) and European Research Council (ERC) under the European Union's Horizon 2020 research and innovation programme (ERC-2014-CoG 'P-MEM-NMR' GA n°648974) is gratefully acknowledged. J.S., K.J. and L.B.A. are supported by individual MSCA incoming fellowships (REA grant agreements n°661799 'COMPLEX-FAST-MAS', n°661175 'virus-DNP-NMR', n°624918 'MEM-MAS')., European Project: 648974,H2020,ERC-2014-CoG,P-MEM-NMR(2015), European Project: 661799,H2020,H2020-MSCA-IF-2014,COMPLEX-fastMAS-NMR(2016), European Project: 661175,H2020,H2020-MSCA-IF-2014,virus-DNP-NMR(2015), European Project: 624918,EC:FP7:PEOPLE,FP7-PEOPLE-2013-IIF,MEM-MAS(2014), 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
Nuclear and High Energy Physics, Fast magic-angle spinning, Analytical chemistry, Protonation, 010402 general chemistry, 01 natural sciences, Spectral line, Nuclear magnetic resonance, Sensitivity, [CHIM.ANAL]Chemical Sciences/Analytical chemistry, Magic angle spinning, Side chain, Protein assemblies, [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM], Nuclear Magnetic Resonance, Biomolecular, Instrumentation, Full protonation, Proton detection, Radiation, Side-chains, 010405 organic chemistry, Chemistry, Fractional deuteration, Proteins, General Chemistry, Deuterium, 0104 chemical sciences, Dilution, Microcrystalline, Solid-state nuclear magnetic resonance, Protons, Resolution, Ultrashort pulse
Abstract

We thank the members of technical staff of ISA for assistance with NMR spectrometers.; International audience; 1H-detection in solid-state NMR of proteins has been traditionally combined with deuteration for both resolution and sensitivity reasons, with the optimal level of proton dilution being dependent on MAS rate. Here we present 1H-detected 15N and 13C CP-HSQC spectra on two microcrystalline samples acquired at 60 and 111 kHz MAS and at ultra-high field. We critically compare the benefits of three labeling schemes yielding different levels of proton content in terms of resolution, coherence lifetimes and feasibility of scalar-based 2D correlations under these experimental conditions. We observe unexpectedly high resolution and sensitivity of aromatic resonances in 2D 13C-1H correlation spectra of protonated samples. Ultrafast MAS reduces or even removes the necessity of 1H dilution for high-resolution 1H-detection in biomolecular solid-state NMR. It yields 15N,1H and 13C,1H fingerprint spectra of exceptional resolution for fully protonated samples, with notably superior 1H and 13C lineshapes for side-chain resonances.

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