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Subpicosecond Spectroscopy of Bacteriorhodopsin
Science, 1978Subpicosecond pulses have been used to study the ultrafast dynamics of the photochemistry of bacteriorhodopsin. An optically induced absorption that appears in about 1.0 picosecond at physiological temperatures has been resolved in time. The data can be interpreted in terms of the photochemical formation of bathobacteriorhodopsin and provide support ...
E P, Ippen +3 more
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Bacteriorhodopsin optoelectronic synapses
Optics Letters, 1997Synapses are critical components of an artificial neural network. Bacteriorhodopsin thin film can be used to construct compact, finely graded synapses for an optoelectronic neural network, based on its photochromic properties. Measurements show that these photochromic changes are blocked at low temperature.
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Photoelectrochemical Cycle of Bacteriorhodopsin
Biochemistry (Moscow), 2001The scheme of the bacteriorhodopsin photocycle associated with a transmembrane proton transfer and electrogenesis is considered. The role of conformational changes in the polypeptide chain during the proton transport is discussed.
I V, Kalaidzidis +3 more
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THE ‘OPSIN SHIFT’ IN BACTERIORHODOPSIN: STUDIES WITH ARTIFICIAL BACTERIORHODOPSINS
Photochemistry and Photobiology, 1981Abstract— The difference (in cm−1) in absorption maxima between the protonated Schiff base of retinals and the pigment derived therefrom has been defined as the opsin shift. It represents the influence of the opsin binding site on the chromophore. The analysis of the opsin shifts of a series of dihydrobacteriorhodopsins has led to the external point ...
Valeria Balogh‐Nair +9 more
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Photoactive bacteriorhodopsin variants
Radiation Physics and Chemistry, 1997Bacteriorhodopsin variants were generated by UV mutagenesis. The protein variants thus engineered were characterized for their UV-visible absorption, light induced proton release activity and photocycle kinetics (BR→M).
SINGH, AK, MAJUMDAR, N, PAVALE, HM
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C(13)-Substituted bacteriorhodopsin analogs
Archives of Biochemistry and Biophysics, 199013-Ethyl-, 13-isopropyl-, 13-tert-butyl-, 13-phenyl-, 13-alpha-naphthyl-, and 13-demethyl-retinals were synthesized and incubated with bacterioopsin (bO) to give the corresponding bacteriorhodopsin (bR) analogs. The capability of the 13-tert-butyl- and 13-alpha-naphthyl-bRs to exist and to photocycle shows that apparently around C(13) of the ...
S V, Danshina +6 more
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Primary photochemical processes in bacteriorhodopsin
Biochemical and Biophysical Research Communications, 1976Abstract Experiments in the picosecond range indicate that the rate of formation of the first intermediate in the photoreaction cycle of bacteriorhodopsin is approximately 1011 sec−1. A transient at 580 nm has been observed and is tentatively attributed to the excited singlet state.
K J, Kaufmann +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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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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