Results 131 to 140 of about 1,270 (179)

Molecular dynamics of bacteriorhodopsin

Journal of Molecular Graphics and Modelling, 1997
A model of bacteriorhodopsin (bR), with a retinal chromophore attached, has been derived for a molecular dynamics simulation. A method for determining atomic coordinates of several ill-defined strands was developed using a structure prediction algorithm based on a sequential Kalman filter technique.
J A, Lupo, R, Pachter
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Snapshots of bacteriorhodopsin

Science, 2016
Structural Biology Bacteriorhodopsin is a membrane protein that harvests the energy content from light to transport protons out of the cell against a transmembrane potential. Nango et al. used timeresolved serial femtosecond crystallography at an x-ray free electron laser to provide 13 structural snapshots of the conformational changes that occur in ...
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Photoelectrochemical Cycle of Bacteriorhodopsin

Biochemistry (Moscow), 2001
The 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, A D, Kaulen, A N, Radionov, L V, Khitrina   +3 more
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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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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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THE ‘OPSIN SHIFT’ IN BACTERIORHODOPSIN: STUDIES WITH ARTIFICIAL BACTERIORHODOPSINS

Photochemistry and Photobiology, 1981
Abstract— 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, John D. Carriker, Barry Honig, Vinayak Kamat, Michael G. Motto, Koji Nakanishi, Ranjan Sen, Mordechai Sheves, Maria Arnaboldi Tanis, Kazuo Tsujimoto   +9 more
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Chromophore mobility in bacteriorhodopsin

Nature, 1977
THE sole protein found in the purple membrane of Halobacterium halobium contains retinal covalently bound by means of a protonated Schiff base linkage to lysine1,2. The only established function of this protein is to act as a light-driven proton pump producing a transmembrane proton gradient, which is coupled to ATP synthesis in the living organism2,3.
W V, Sherman, S R, Caplan
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Photoaffinity labeling of bacteriorhodopsin

Biochemistry, 1990
14C-Labeled optically pure 3S- and 3R-(diazoacetoxy)-all-trans-retinals were incorporated separately into bacterioopsin to reconstitute functional bacteriorhodopsin (bR) analogues, 3S- and 3R-diazo-bRs. UV irradiation at 254 nm generated highly reactive carbenes, which cross-linked the radiolabeled retinals to amino acid residues in the vicinity of the
W D, Ding, A, Tsipouras, H, Ok, T, Yamamoto, M A, Gawinowicz, K, Nakanishi   +5 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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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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