Results 81 to 90 of about 1,182 (121)

A Review on Low-Dimensional Nanoarchitectonics for Neurochemical Sensing and Modulation in Responsive Neurological Outcomes. [PDF]

Biomolecules
Tabish M, Malik I, Akhtar A, Afzal M.
europepmc   +1 more source

Comparative genomics of the highly halophilic Haloferacaceae. [PDF]

Sci Rep
Griffiths DB, Tiwari RP, Murphy DV, Scott C.   +3 more
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Light cues drive community-wide transcriptional shifts in the hypersaline South Bay Salt Works. [PDF]

Commun Biol
Weng MM, Klempay B, Bowman JS, Fisher L, Camplong C, Doran PT, Rundell S, Glass JB, Dutta A, Pontefract A, Bartlett DH, Schmidt B, Johnson SS.   +12 more
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Extremophiles in a changing world. [PDF]

Extremophiles
Cowan DA, Albers SV, Antranikian G, Atomi H, Averhoff B, Basen M, Driessen AJM, Jebbar M, Kelman Z, Kerou M, Littlechild J, Müller V, Schönheit P, Siebers B, Vorgias K.   +14 more
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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
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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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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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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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Phylogenetic relationships among bacteriorhodopsins

Research in Microbiology, 1994
Retinal-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.
G, Kuan, M H, Saier
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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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