Results 81 to 90 of about 1,206 (141)
Retinal photoisomerization versus counterion protonation in light and dark-adapted bacteriorhodopsin and its primary photoproduct. [PDF]
Malakar P +6 more
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Declines in ice cover are accompanied by light limitation responses and community change in freshwater diatoms. [PDF]
Zepernick BN +11 more
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Mid-day photomixotrophy by <i>Roseiflexus</i> spp. and implications for the <sup>13</sup>C content of hot spring cyanobacterial mats. [PDF]
Moran JJ +7 more
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Comparative genomics of the highly halophilic Haloferacaceae. [PDF]
Griffiths DB +3 more
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Conformational Flexibility of Transmembrane Helices: How it Works and Where it Matters. [PDF]
Langosch D.
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Photoreactions of bacteriorhodopsin
Biophysics of Structure and Mechanism, 1977Bacteriorhodopsin 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 +2 more
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Molecular dynamics of bacteriorhodopsin
Journal of Molecular Graphics and Modelling, 1997A 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, 2016Structural 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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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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