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          Institute: MPI für Biophysik     Collection: Abt. Strukturbiologie     Display Documents

ID: 571444.0, MPI für Biophysik / Abt. Strukturbiologie
Amphipols From A to Z
Authors:Popot, J.-L.; Althoff, T.; Bagnard, D.; Banères, J.-L.; Bazzacco, P.; Billon-Denis, E.; Catoire, L. J.; Champeil, P.; Charvolin, D.; Cocco, M.-J.; Crémel, G.; Dahmane, T.; de la Maza, L. M.; Ebel, C.; Gabel, F.; Giusti, F.; Gohon, Y.; Goormaghtigh, E.; Guittet, E.; Kleinschmidt, J. H.; Kühlbrandt, W.; Le Bon, C.; Martinez, K. L.; Picard, M.; Pucci, B.; Sachs, J. N.; Tribet, C.; van Heijenoort, C.; Wien, F.; Zito, F.; Zoonens, M.
Date of Publication (YYYY-MM-DD):2011
Title of Journal:Annual Review of Biophysics
Journal Abbrev.:Annu. Rev. Biophys.
Start Page:379
End Page:408
Review Status:Peer-review
Audience:Experts Only
Abstract / Description:Amphipols (APols) are short amphipathic polymers that can substitute for detergents to keep integral membrane proteins (MPs) water soluble. In this review, we discuss their structure and solution behavior; the way they associate with MPs; and the structure, dynamics, and solu- tion properties of the resulting complexes. All MPs tested to date form water-soluble complexes with APols, and their biochemical stability is in general greatly improved compared with MPs in detergent solutions. The functionality and ligand-binding properties of APol-trapped MPs are reviewed, and the mechanisms by which APols stabilize MPs are discussed. Applications of APols include MP folding and cell-free synthesis, structural studies by NMR, electron microscopy and X-ray diffraction, APol-mediated immobilization of MPs onto solid supports, proteomics, delivery of MPs to preexisting membranes, and vaccine formulation.
Free Keywords:membrane proteins; amphipathic polymers; membrane biophysics; membrane biochemistry
External Publication Status:published
Document Type:Article
Communicated by:N. N.
Affiliations:MPI für Biophysik/Abteilung Strukturbiologie
External Affiliations:Institut de Biologie Physico-Chimique, CNRS/Université Paris-7 UMR 7099, F-75005 Paris, France;
Université ́ de Strasbourg, INSERM U682, F-67084 Strasbourg, France;
Institut des Biomolécules Max Mousseron, CNRS/Universités Montpellier I & II UMR 5247, F-34093 Montpellier, France;
Institut de Biologie et de Technologies de Saclay, CEA/SB2SM and CNRS/URA 2096, F-91191 Gif-sur-Yvette Cedex, France;
Department of Molecular Biology and Biochemistry, University of California, Irvine, California 92697-3900;
Centre de Neurochimie, INSERM U682, F-67084 Strasbourg, France;
Institut de Biologie Physico-Chimique, CNRS/Université Paris-7 UMR 7099, F-75005 Paris, France;
Department of Pathology and Laboratory Medicine Medical Sciences I, University of California, Irvine, California 92697-4800;
Institut de Biologie Structurale, CEA/CNRS/UJF UMR5075, F-38027 Grenoble, France;
Institut de Biologie Physico-Chimique, CNRS/Université Paris-7 UMR 7099, F-75005 Paris, France; Unité de Chimie Biologique, AgroParisTech/INRA, F-78850 Thiverval-Grignon, France;
Center for Structural Biology and Bioinformatics, Université Libre de Bruxelles, B-10050 Bruxelles, Belgium;
Institut de Chimie des Substances Naturelles, CNRS UPR 2301, F-91198 Gif-sur-Yvette, France;
Fachbereich Biologie, Universität Konstanz, D-78457 Konstanz, Germany;
Department of Neuroscience and Pharmacology & Nanoscience Center, University of Copenhagen, DK-2100 Copenhagen, Denmark;
Institut de Biologie Physico-Chimique, CNRS/Université Paris-7 UMR 7099, F-75005 Paris, France;
Laboratoire de Chimie Bioorganique et des Systèmes Moléculaires Vectoriels, Université d’Avignon et des Pays de Vaucluse, F-84000 Avignon, France;
Department of Biomedical Engineering, University of Minnesota, Minneapolis, Minnesota 55455;
Département de Chimie, CNRS/ENS/Université Paris-6 UMR 8640, Ecole Normale Supérieure, F-75005 Paris;
DISCO, Synchrotron Soleil, F-91192 Gif-sur-Yvette, France
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