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The Use of Amphipols for Solution NMR Studies of Membrane Proteins: Advantages and Constraints as Compared to Other Solubilizing Media |
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| Authors: | Noelya Planchard Élodie Point Tassadite Dahmane Fabrice Giusti Marie Renault Christel Le Bon Grégory Durand Alain Milon Éric Guittet Manuela Zoonens Jean-Luc Popot Laurent J. Catoire |
| Affiliation: | 1. Laboratoire de Biologie Physico-Chimique des Protéines Membranaires, Institut de Biologie Physico-Chimique (FRC 550), UMR 7099, CNRS, Université Paris 7, 13 rue Pierre et Marie Curie, 75005, Paris, France 2. Centre de Versailles-Grignon, Institut Jean-Pierre Bourgin, UMR 1318 INRA-AgroParisTech, Batiment 7, INRA, Route de St-Cyr, 78026, Versailles Cedex, France 3. Department of Biochemistry and Molecular Biophysics, Columbia University, 650 West 168th Street, 202 BB, New York, NY, 10032, USA 4. Laboratoire de RMN et des interactions protéines/membranes, CNRS, Institut de Pharmacologie et de Biologie Structurale, 205 route de Narbonne, BP64182, 31077, Toulouse, France 5. Equipe Chimie Bioorganique et Systèmes Amphiphiles, Université d’Avignon et des Pays de Vaucluse, 33 rue Louis Pasteur, 84000, Avignon, France 6. Institut des Biomolécules Max Mousseron (UMR 5247), 15 avenue Charles Flahault, 34093, Montpellier Cedex 05, France 7. Centre de Recherche de Gif, Laboratoire de Chimie et Biologie Structurales, UPR 2301 CNRS, ICSN, 91198, Gif-sur-Yvette, France |
| Abstract: | Solution-state nuclear magnetic resonance studies of membrane proteins are facilitated by the increased stability that trapping with amphipols confers to most of them as compared to detergent solutions. They have yielded information on the state of folding of the proteins, their areas of contact with the polymer, their dynamics, water accessibility, and the structure of protein-bound ligands. They benefit from the diversification of amphipol chemical structures and the availability of deuterated amphipols. The advantages and constraints of working with amphipols are discussed and compared to those associated with other non-conventional environments, such as bicelles and nanodiscs. |
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