Asymmetric Structure of the Purple Membrane
- 3 June 1977
- journal article
- research article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 196 (4294) , 1101-1104
- https://doi.org/10.1126/science.870970
Abstract
There is both functional and structural evidence that bacteriorhodopsin is oriented asymmetrically across the purple membrane of Halobacterium halobium. To assess the degree of asymmetry, the x-ray diffraction data from the membrane have been analyzed for possible electron-density profiles. A recent theory predicts that only a limited number of profiles are consistent with the continuous diffraction data, and two possible profiles have been found. Both profiles indicate that the protein molecules span a lipid bilayer in the membrane. Both profiles are asymmetric; there are more lipid molecules in one half of the membrane than in the other, and the bacteriorhodopsin molecule shows a slight complementary asymmetry.This publication has 5 references indexed in Scilit:
- Three-dimensional model of purple membrane obtained by electron microscopyNature, 1975
- The structure of the purple membrane from Halobacterium halobium: Analysis of the X-ray diffraction patternJournal of Molecular Biology, 1975
- Bacteriorhodopsin: A trans-membrane pump containing α-helixJournal of Molecular Biology, 1975
- Direct structure determination of asymmetric membrane systems from X-ray diffractionActa Crystallographica Section A, 1975
- Functions of a New Photoreceptor MembraneProceedings of the National Academy of Sciences, 1973