Contrast-Matched Isotropic Bicelles: A Versatile Tool to Specifically Probe the Solution Structure of Peripheral Membrane Proteins Using SANS
العنوان: | Contrast-Matched Isotropic Bicelles: A Versatile Tool to Specifically Probe the Solution Structure of Peripheral Membrane Proteins Using SANS |
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المؤلفون: | Liza Mouret, Olivier Delalande, Marie-Sousai Appavou, Jean-François Hubert, Raphael Dos Santos Morais, Anne Martel, Sophie Combet, Elisabeth Le Rumeur, Arnaud Bondon, Javier Pérez |
المساهمون: | Institut de Génétique et Développement de Rennes (IGDR), Université de Rennes (UR)-Centre National de la Recherche Scientifique (CNRS)-Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique ), Laboratoire Léon Brillouin (LLB - UMR 12), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Synchrotron SOLEIL, Institut des Sciences Chimiques de Rennes (ISCR), Université de Rennes (UR)-Institut National des Sciences Appliquées - Rennes (INSA Rennes), Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Ecole Nationale Supérieure de Chimie de Rennes (ENSCR)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Institut Laue-Langevin (ILL), Jülich Centre for Neutron Science (JCNS), Forschungszentrum Jülich GmbH | Centre de recherche de Juliers, Helmholtz-Gemeinschaft = Helmholtz Association-Helmholtz-Gemeinschaft = Helmholtz Association, Association Fran?aise contre les Myopathies, Conseil R?gional de Bretagne, Synchrotron Soleil, Laboratoire L?on-Brillouin, Université de Rennes 1 (UR1), Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES)-Centre National de la Recherche Scientifique (CNRS)-Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique ), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)-Université Paris-Saclay, Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC)-Université de Rennes 1 (UR1), Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES)-Ecole Nationale Supérieure de Chimie de Rennes (ENSCR)-Institut National des Sciences Appliquées - Rennes (INSA Rennes), Institut National des Sciences Appliquées (INSA)-Université de Rennes (UNIV-RENNES)-Institut National des Sciences Appliquées (INSA), ILL, Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique )-Centre National de la Recherche Scientifique (CNRS)-Université de Rennes 1 (UR1), Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES), Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES)-Institut National des Sciences Appliquées - Rennes (INSA Rennes), Institut National des Sciences Appliquées (INSA)-Université de Rennes (UNIV-RENNES)-Institut National des Sciences Appliquées (INSA)-Ecole Nationale Supérieure de Chimie de Rennes (ENSCR)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS) |
المصدر: | Langmuir Langmuir, 2017, 33 (26), pp.6572-6580. ⟨10.1021/acs.langmuir.7b01369⟩ Langmuir, American Chemical Society, 2017, 33 (26), pp.6572-6580. ⟨10.1021/acs.langmuir.7b01369⟩ |
بيانات النشر: | American Chemical Society (ACS), 2017. |
سنة النشر: | 2017 |
مصطلحات موضوعية: | 0301 basic medicine, Magnetic Resonance Spectroscopy, Model lipid bilayer, Neutron scattering, Membrane Lipids, 03 medical and health sciences, X-Ray Diffraction, Scattering, Small Angle, Electrochemistry, Humans, General Materials Science, Spectroscopy, [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM], Chemistry, Small-angle X-ray scattering, Peripheral membrane protein, Membrane Proteins, Surfaces and Interfaces, Nuclear magnetic resonance spectroscopy, Condensed Matter Physics, Crystallography, 030104 developmental biology, Membrane, Membrane protein, Solid-state nuclear magnetic resonance, Chemical physics |
الوصف: | International audience; Obtaining structural information on integral or peripheral membrane proteins is currently arduous due to the difficulty of their solubilization, purification, and crystallization (for X-ray crystallography (XRC) application). To overcome this challenge, bicelles are known to be a versatile tool for high-resolution structure determination, especially when using solution and/or solid state nuclear magnetic resonance (NMR) and, to a lesser extent, XRC. For proteins not compatible with these high-resolution methods, small-angle X-ray and neutron scattering (SAXS and SANS, respectively) are powerful alternatives to obtain structural information directly in solution. In particular, the SANS-based approach is a unique technique to obtain low-resolution structures of proteins in interactions with partners by contrast-matching the signal coming from the latter. In the present study, isotropic bicelles are used as a membrane mimic model for SANS-based structural studies of bound peripheral membrane proteins. We emphasize that the SANS signal coming from the deuterated isotropic bicelles can be contrast-matched in 100% D2O-based buffer, allowing us to separately and specifically focus on the signal coming from the protein in interaction with membrane lipids. We applied this method to the DYS-R11-15 protein, a fragment of the central domain of human dystrophin known to interact with lipids, and we were able to recover the signal from the protein alone. This approach gives rise to new perspectives to determine the solution structure of peripheral membrane proteins interacting with lipid membranes and might be extended to integral membrane proteins. |
تدمد: | 1520-5827 0743-7463 |
DOI: | 10.1021/acs.langmuir.7b01369 |
DOI: | 10.1021/acs.langmuir.7b01369⟩ |
URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b8348db317b98968d112c1f883777fcd https://doi.org/10.1021/acs.langmuir.7b01369 |
Rights: | OPEN |
رقم الانضمام: | edsair.doi.dedup.....b8348db317b98968d112c1f883777fcd |
قاعدة البيانات: | OpenAIRE |
تدمد: | 15205827 07437463 |
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DOI: | 10.1021/acs.langmuir.7b01369 |