Results 181 to 190 of about 9,873 (221)
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1987
Bacteriorhodopsin is an integral membrane protein found in the purple membrane of halobacterium halobium. Since electron microscopy data (Henderson and Unwin, 1975) established that the membrane- imbedded part of bacteriorhodopsin consists of seven closely packed α-helices there has been much interest in learning what parts of the amino acid sequence ...
Leslie A. Kuhn, John S. Leigh
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Bacteriorhodopsin is an integral membrane protein found in the purple membrane of halobacterium halobium. Since electron microscopy data (Henderson and Unwin, 1975) established that the membrane- imbedded part of bacteriorhodopsin consists of seven closely packed α-helices there has been much interest in learning what parts of the amino acid sequence ...
Leslie A. Kuhn, John S. Leigh
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Biogenesis of bacteriorhodopsin
Journal of Protein Chemistry, 1989P, Wrede +3 more
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Bacteriorhodopsin and Rhodopsin
2007The sections in this article are 1 Introduction 2 NMR Strategies 3 Structure 4 Protonation and Hydrogen Bonding 5 Proton Diffusion 6 Biographical Sketch Related ...
Judith Herzfeld, Jingui G. Hu
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Nature, 2000
For 30 years and more, the mechanism of a microbial proton pump has been subject to increasingly sophisticated analysis. The full picture of how the pump operates is now emerging.
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For 30 years and more, the mechanism of a microbial proton pump has been subject to increasingly sophisticated analysis. The full picture of how the pump operates is now emerging.
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On the Folding of Bacteriorhodopsin
1986A great deal of effort has been expended in trying to understand the folding of soluble proteins, the tertiary structures of which have been determined in many cases. The problem has turned out to be very complex, and the current lines of study have met with only limited success.
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Functions of Bacteriorhodopsin
1974Our results indicate that the bacteriorhodopsin in Halobacterium halobium has not only an energy-converting function as reported by Oesterhelt (see p.69ff), but also a photosensory function comparable with the photoreception in animals (Hildebrand and Dencher, in preparation).
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