Results 121 to 130 of about 1,651 (181)
Conformational Flexibility of Transmembrane Helices: How it Works and Where it Matters. [PDF]
Langosch D.
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Retinal photoisomerization versus counterion protonation in light and dark-adapted bacteriorhodopsin and its primary photoproduct. [PDF]
Malakar P +6 more
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Comparative genomics of the highly halophilic Haloferacaceae. [PDF]
Griffiths DB +3 more
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A Review on Low-Dimensional Nanoarchitectonics for Neurochemical Sensing and Modulation in Responsive Neurological Outcomes. [PDF]
Tabish M, Malik I, Akhtar A, Afzal M.
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Light cues drive community-wide transcriptional shifts in the hypersaline South Bay Salt Works. [PDF]
Weng MM +12 more
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Phylogenetic relationships among bacteriorhodopsins
Research in Microbiology, 1994Retinal-containing proteins of archaea comprise a single family of homologous proteins that fall into three clusters correlating with function: the proton-transporting bacteriorhodopsins, the chloride-transporting halorhodopsins and the colour-discriminating sensory rhodopsins.
Milton H Saier Jr
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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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Photoaffinity labeling of bacteriorhodopsin
Biochemistry, 199014C-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 +5 more
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Chromophore mobility in bacteriorhodopsin
Nature, 1977THE 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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