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Site-directed mutagenesis of an energy transducing protein: Bacteriorhodopsin. Final report, July 15, 1992--July 14, 1996
Author(s) -
Richard Needleman
Publication year - 1998
Language(s) - English
Resource type - Reports
DOI - 10.2172/661520
Subject(s) - bacteriorhodopsin , proton , mutagenesis , coupling (piping) , mutant , biophysics , mechanism (biology) , chemistry , biology , stereochemistry , physics , biochemistry , materials science , nuclear physics , gene , membrane , metallurgy , quantum mechanics
The objective was to understand at the molecular level how bacteriorhodopsin (BR) transports protons. The work involves the synthesis of mutant BRs, their expression in the natural host, H. halobium, and an investigation of their photocycles. This final report has led to the development of a greatly improved expression system and to an increased understanding of the mechanism of proton transport. At the beginning of the award period a central concern was establishing the details of the photocycle. This phase was essentially complete by mid 1994. The author then investigated the energy coupling mechanism which allows uni-directional proton transfer and found that a major determinant was the coupling of the proton release to changes in the pKa of D85

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