Studies of bacteriorhodopsin over the past fourteen years have contributed in a special special way to our present understanding of ionic pumps and membrane proteins in general. This is because bacteriorhodopsin, a light driven proton pump found in the halo bacteria, is a small membrane protein that contains the minimum features required for active proton transloca tion; many other systems are larger proteins and show considerable structural complexity. Because bacteriorhodopsin is in a crystalline array, it was the first membrane protein for which a three-dimensional structure could be determined. The resulting characteristic bacteriorhodopsin struc ture served as a test model for various strategies designed to predict and evaluate the structure of other membrane proteins. It has become evident in the last few years, however, that the halo bacteria contain other retinal proteins that are potentially as interesting as bacteriorhodopsin. One of
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Janos Κ. Lanyi (1986) studied this question.