Results 111 to 120 of about 5,006 (168)

Elektronentransport in nanoskaligen Bacteriorhodopsin-Übergangen

This dissertation investigates electron transport across junctions comprising electrostatically coupled bacteriorhodopsin multilayers. A weak dependence of the conductance on layer thickness and temperature was measured, possibly suggesting transport ...
Chryssikos, Demetrios-Domenikos
core  

Quantum dot enhancement of bacteriorhodopsin-based electrodes

Biosensors and Bioelectronics, 2010
Nanoscale sensing arrays utilizing the unique properties of the optical protein bacteriorhodopsin and colloidal semiconductor quantum dots are being developed for toxin detection applications.
Mark H Griep, Eric M Winder, Craig Friedrich   +2 more
exaly   +2 more sources

Bleaching of bacteriorhodopsin by continuous light [PDF]

FEBS Letters, 1999
A new two step photobleaching process is observed under continuous illumination of bacteriorhodopsin. This photobleaching is considerable even at physiological temperatures and becomes large at 50–60°C.
András Dér, Z Tokaji
exaly   +2 more sources

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Photoreactions of bacteriorhodopsin

Biophysics of Structure and Mechanism, 1977
Bacteriorhodopsin is a membrane-bound light energy transducer which generates an electrochemical proton gradient. It undergoes a cyclic photoreaction in which five intermediates have been identified. During the cycle it releases a proton from one surface of the membrane and takes up a proton on the opposite surface.
W, Stoeckenius, R H, Lozier, W, Niederberger   +2 more
openaire   +2 more sources

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
openaire   +2 more sources

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 ...
openaire   +2 more sources

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
openaire   +2 more sources

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
openaire   +2 more sources

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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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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