Results 141 to 150 of about 1,270 (179)
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The Photocycles of Bacteriorhodopsin

Israel Journal of Chemistry, 1995
AbstractThe photoisomerization of all‐trans‐retinal of bacteriorhodopsin to 13‐cisgives rise to a series of unstable states that thermally interconvert on the picosecond to millisecond timescale, and ultimately decay back to the initial state. Since this “photocycle” drives the translocation of a proton from the cytoplasmic to the extracellular side of
Janos K. Lanyi, György Váró
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PHOTODESTRUCTION OF BACTERIORHODOPSIN

Photochemistry and Photobiology, 1991
Abstract— Suspensions of purple membrane fragments showed obvious signs of degradation after illumination with intense pulses of light from 10 ns frequency doubled Nd: YAG laser at 532 nm with intensity densities in excess of 1 MW/cm2. Using controlled illumination, a small fraction of the bacteriorhodopsin protein molecules were randomly destroyed in
JÓAZSEF CZÉAGÉA, LOU REINISCH
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Biogenesis of bacteriorhodopsin

Journal of Protein Chemistry, 1989
P, Wrede   +3 more
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The Bacteriorhodopsin Puzzle

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 — the movie

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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Bacteriorhodopsin and Rhodopsin

2007
The 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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On the Folding of Bacteriorhodopsin

1986
A 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

1974
Our 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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