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BP: Fachverband Biologische Physik
BP 13: Posters: Biological Membranes
BP 13.11: Poster
Montag, 14. März 2011, 17:15–20:00, P3
Crystallinity of purple membranes comprising the chloride-pumping bacteriorhodopsin variant D85T — •Daniel Rhinow1, Ivan Chizhic2, Roelf-Peter Baumann2, Frank Noll2, and Norbert Hampp2 — 1Max-Planck-Institut für Biophysik, Max-von-Laue-Str. 3, 60438 Frankfurt — 2Philipps-Universität Marburg, Fachbereich Chemie, Hans-Meerwein-Str., 35032 Marburg
Purple membranes (PM) from Halobacterium salinarum comprise bacteriorhodopsin (BR) and lipids only and form a 2-D crystalline lattice in the cell membrane. In PMs comprising the chloride-pumping BR-variant D85T we have observed a tuneable tendency to form crystalline domains, which depends on pH-value and chloride ion concentration. We have combined small angle X-ray scattering, atomic force microscopy and freeze-fracture electron microscopy to analyze structural transitions within PM-D85T statistically as well as on the single membrane level. PM-D85T is a model system to study membrane protein association upon substrate binding in a native environment.