Results 121 to 130 of about 5,006 (168)

Structure and function of bacteriorhodopsin

Advances in Biophysics, 1988
Bacteriorhodopsin (bR) is a powerful light-driven proton pump. We have developed a procedure to prepare bR-containing membrane vesicles in which a pH gradient as large as 4 pH units can be generated and maintained in the light. Using such a system, we have demonstrated that bR exhibits a high proton pump activity in a wide pH region; it works well at ...
T, Kouyama, K, Kinosita, A, Ikegami
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Reorientations in the Bacteriorhodopsin Photocycle

Biochemistry, 1994
Reversible photoinduced reorientations of bacteriorhodopsin have been detected in suspensions of the purple membrane of Halobacterium salinarium. The anisotropy in bacteriorhodopsin during the nanosecond through millisecond stages of the photocycle was measured by time-resolved linear dichroism and transient absorption measurements.
Q, Song, G S, Harms, C, Wan, C K, Johnson   +3 more
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Subpicosecond Spectroscopy of Bacteriorhodopsin

Science, 1978
Subpicosecond 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, C V, Shank, A, Lewis, M A, Marcus   +3 more
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Bacteriorhodopsin optoelectronic synapses

Optics Letters, 1997
Synapses 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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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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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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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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Biogenesis of bacteriorhodopsin

Journal of Protein Chemistry, 1989
P, Wrede, M, Lange, G, Büldt, U, Frevert   +3 more
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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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