Lipid-bilayers membranes produce water-impermeable barriers that define the boundaries of biological cells and of specialized compartments within these cells. Protein molecules embedded into or intimately associated with the lipid bilayer control communication and transport across biological membranes. Both external surfaces of a lipid bilayer are hydrophilic, but the bilayer interior is hydrophobic as it is composed from aliphatic chains. Accordingly, protein molecules embedded into a membrane have hydrophobic surfaces in association with the lipids and, typically, hydrophilic portions that protrude from the membrane surface. Such protein molecules are not directly soluble in aqueous media and hence require detergents to cover the hydrophobic surfaces during extraction, solubilization and purification. It is primarily for this reason that integral membrane proteins present formidable, but not insurmountable obstacles to structural and other analyses. Early stages of any project requiring purified protein can be greatly assisted with the use of high-throughput approaches. The initial cloning, expression trials and optimization of purification methods and conditions are particularly well-suited for automated techniques. COMPP is in the unique position of being able to rely on ten years of experience with the New York Consortium of Membrane Protein Structure, therefore, it will be able to offer services and engage in collaborations from the first day of operation. Furthermore, COMPP will continue to develop reagents and methods for the efficient production, sample preparation, functional analyses and structure determination of membrane proteins. These will be made as services as soon as they have been tested in collaborative projects. We propose to make all of these membrane-protein related resources available not just to the structural biology community, but to scientists of all disciplines.
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| Liu, Qun; Hendrickson, Wayne A (2017) Contemporary Use of Anomalous Diffraction in Biomolecular Structure Analysis. Methods Mol Biol 1607:377-399 |
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| Clarke, Oliver B; Hendrickson, Wayne A (2016) Structures of the colossal RyR1 calcium release channel. Curr Opin Struct Biol 39:144-152 |
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