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Novel Tripod Amphiphiles for Membrane Protein Analysis
Authors:Prof Pil Seok Chae  Andrew C Kruse  Dr Kamil Gotfryd  Rohini R Rana  Kyung Ho Cho  Prof Søren G F Rasmussen  Hyoung Eun Bae  Richa Chandra  Prof Ulrik Gether  Prof Lan Guan  Prof Brian K Kobilka  Prof Claus J Loland  Dr Bernadette Byrne  Prof Samuel H Gellman
Institution:1. Department of Bionano Engineering, Hanyang University Ansan, 426‐791 (Korea), Fax: (+81)?31‐436‐8146;2. Molecular and Cellular Physiology, Stanford University, CA 94305 (USA);3. Department of Neuroscience and Pharmacology, University of Copenhagen, 2200 Copenhagen (Denmark);4. Department of Life Sciences, Imperial College London, SW7 2AZ (UK);5. Department of Cell Physiology and Molecular Biophysics, Texas Tech University Health Sciences Center, Lubbock, TX 79430 (USA);6. Department of Chemistry, University of Wisconsin‐Madison, 1101 University Avenue, Madison, WI 53706 (USA)
Abstract:Integral membrane proteins play central roles in controlling the flow of information and molecules across membranes. Our understanding of membrane protein structures and functions, however, is seriously limited, mainly due to difficulties in handling and analysing these proteins in aqueous solution. The use of a detergent or other amphipathic agents is required to overcome the intrinsic incompatibility between the large lipophilic surfaces displayed by the membrane proteins in their native forms and the polar solvent molecules. Here, we introduce new tripod amphiphiles displaying favourable behaviours toward several membrane protein systems, leading to an enhanced protein solubilisation and stabilisation compared to both conventional detergents and previously described tripod amphiphiles.
Keywords:amphiphiles  membrane proteins  molecular design  protein structures  stabilization
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