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1. Lipid bilayer-bound conformation of an integral membrane beta barrel protein by multidimensional MAS NMR

Author

Yongchao Su, Robert Silvers, Guido Pintacuda, Robert G. Griffin, Lyndon Emsley, Lindsay Clark, Loren B. Andreas, Matthew T. Eddy, Gerhard Wagner, Massachusetts Institute of Technology. Department of Chemistry, Francis Bitter Magnet Laboratory (Massachusetts Institute of Technology), Griffin, Robert Guy, Eddy, Matthew Thomas, Su, Yongchao, Silvers, Robert, Andreas, Loren, Clark, Lindsay, Department of Chemistry [MIT Cambridge], Massachusetts Institute of Technology (MIT), Francis Bitter Magnet Lab, 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), Dept Biol Chem & Mol Pharmacol, Harvard University [Cambridge], Solid-State NMR Methods for Materials - Méthodes de RMN à l'état solide pour les matériaux, and NIH Grants EB001960 and EB002026.

Subjects
Models, Molecular, Protein Folding, Lipid Bilayers, 010402 general chemistry, 01 natural sciences, Biochemistry, Protein Structure, Secondary, Article, CHIMERIC POTASSIUM CHANNEL, 03 medical and health sciences, Protein structure, [CHIM.ANAL]Chemical Sciences/Analytical chemistry, Magic angle spinning, Membrane fluidity, Humans, NICOTINIC ACETYLCHOLINE-RECEPTOR, Lipid bilayer, Nuclear Magnetic Resonance, Biomolecular, Integral membrane protein, Micelles, Spectroscopy, 030304 developmental biology, 0303 health sciences, VDAC, Chemistry, Voltage-Dependent Anion Channel 1, PHOSPHOLAMBAN PENTAMER, ANION-SELECTIVE CHANNEL, MITOCHONDRIAL OUTER-MEMBRANE, Magnetic Resonance Imaging, TRANSMEMBRANE DOMAIN, Protein Structure, Tertiary, SOLID-STATE NMR, 2D lipid crystals, 3. Good health, 0104 chemical sciences, Crystallography, ANGLE-SPINNING NMR, MAS, Beta barrel, Solid-state nuclear magnetic resonance, Membrane protein, BACTERIORHODOPSIN PHOTOCYCLE, Recoupling, lipids (amino acids, peptides, and proteins), ROTATIONAL RESONANCE
Abstract

The human voltage dependent anion channel 1 (VDAC) is a 32 kDa β-barrel integral membrane protein that controls the transport of ions across the outer mitochondrial membrane. Despite the determination of VDAC solution and diffraction structures, a structural basis for the mechanism of its function is not yet fully understood. Biophysical studies suggest VDAC requires a lipid bilayer to achieve full function, motivating the need for atomic resolution structural information of VDAC in a membrane environment. Here we report an essential step toward that goal: extensive assignments of backbone and side chain resonances for VDAC in DMPC lipid bilayers via magic angle spinning nuclear magnetic resonance (MAS NMR). VDAC reconstituted into DMPC lipid bilayers spontaneously forms two-dimensional lipid crystals, showing remarkable spectral resolution (0.5–0.3 ppm for [superscript 13]C line widths and, National Institutes of Health (U.S.) (Grant EB001960), National Institutes of Health (U.S.) (Grant EB002026)

Published
2015
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2. Efficient cross-effect dynamic nuclear polarization without depolarization in high-resolution MAS NMR

Author

Anne-Laure Barra, Gaël De Paëpe, Guinevere Mathies, Frederic Mentink-Vigier, Sabine Hediger, Yangping Liu, Daniel Lee, Robert G. Griffin, Marc A. Caporini, Magnetic Resonance (RM ), Modélisation et Exploration des Matériaux (MEM), 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)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), MIT - Francis Bitter Magnet Lab, Massachusetts Institute of Technology (MIT), Tianjin University (TJU), Laboratoire national des champs magnétiques intenses - Grenoble (LNCMI-G ), Institut National des Sciences Appliquées - Toulouse (INSA Toulouse), Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-Institut National des Sciences Appliquées (INSA)-Université de Toulouse (UT)-Université Toulouse III - Paul Sabatier (UT3), Université de Toulouse (UT)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019]), Bruker BioSpin [Billerica, MA], Centre National de la Recherche Scientifique (CNRS), ANR-12-BS08-0016,CryoMAS4DNP,Polarisation dynamique nucléaire en rotation à l'angle magique à très basse température et à haut champ magnétique(2012), ANR-11-LABX-0003,ARCANE,Grenoble, une chimie bio-motivée(2011), ANR-10-EQPX-0047,SENS,RMN de Surface Exalté par Polarisation Dynamique Nucléaire(2010), European Project: 682895, Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019]), Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Université Toulouse III - Paul Sabatier (UT3), and Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])

Subjects
Cross effect, 010405 organic chemistry, Chemistry, [PHYS.PHYS.PHYS-ATM-PH]Physics [physics]/Physics [physics]/Atomic and Molecular Clusters [physics.atm-clus], Analytical chemistry, High resolution, Natural abundance, Depolarization, General Chemistry, 010402 general chemistry, Polarization (waves), 01 natural sciences, 0104 chemical sciences, Magnetic field, Atomic resolution, Chemical physics, ddc:540, Spinning, ComputingMilieux_MISCELLANEOUS
Abstract

The mixed trityl-TEMPO biradical TEMTriPol-1 provides excellent MAS NMR sensitivity with DNP while avoiding nuclear depolarization., Dynamic nuclear polarization (DNP) has the potential to enhance the sensitivity of magic-angle spinning (MAS) NMR by many orders of magnitude and therefore to revolutionize atomic resolution structural analysis. Currently, the most widely used approach to DNP for studies of chemical, material, and biological systems involves the cross-effect (CE) mechanism, which relies on biradicals as polarizing agents. However, at high magnetic fields (≥5 T), the best biradicals used for CE MAS-DNP are still far from optimal, primarily because of the nuclear depolarization effects they induce. In the presence of bisnitroxide biradicals, magic-angle rotation results in a reverse CE that can deplete the initial proton Boltzmann polarization by more than a factor of 2. In this paper we show that these depolarization losses can be avoided by using a polarizing agent composed of a narrow-line trityl radical tethered to a broad-line TEMPO. Consequently, we show that a biocompatible trityl-nitroxide biradical, TEMTriPol-1, provides the highest MAS NMR sensitivity at ≥10 T, and its relative efficiency increases with the magnetic field strength. We use numerical simulations to explain the absence of depolarization for TEMTriPol-1 and its high efficiency, paving the way for the next generation of polarizing agents for DNP. We demonstrate the superior sensitivity enhancement using TEMTriPol-1 by recording the first solid-state 2D 13C–13C correlation spectrum at natural isotopic abundance at a magnetic field of 18.8 T.

Published
2017
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