Results 121 to 130 of about 1,294 (176)

Molecular Force Modulation Spectroscopy Revealing the Dynamic Response of Single Bacteriorhodopsins [PDF]

Biophysical Journal, 2005
Recent advances in atomic force microscopy allowed globular and membrane proteins to be mechanically unfolded on a single-molecule level. Presented is an extension to the existing force spectroscopy experiments.
Harald Janovjak, Müller Dj
exaly   +2 more sources

Bacteriorhodopsins as Optoelectronic Materials

, 1998
Nikolai Vsevolodov
exaly   +2 more sources

PHOTOCHEMICAL STUDIES OF ARTIFICIAL BACTERIORHODOPSINS

Photochemistry and Photobiology, 1983
M. Ottolenghi, P. Umadevi, M. SHEVES, V. Rosenbach   +3 more
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

The Unique Properties of Bacteriorhodopsins as Energy Converters

, 1998
Nikolai Vsevolodov
exaly   +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 ...
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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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P-E3-18 Early charge separation in modified bacteriorhodopsins

Progress in Biophysics and Molecular Biology, 1996
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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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