bacteriorhodopsin


Also found in: Medical, Acronyms, Encyclopedia, Wikipedia.

bac·te·ri·o·rho·dop·sin

 (băk-tîr′ē-ō-rō-dŏp′sĭn)
n.
A pigmented membrane protein found in extremely halophilic archaea of the genus Halobacterium that converts light energy to chemical energy and is structurally similar to rhodopsin.

bac•te•ri•o•rho•dop•sin

(bækˌtɪər i oʊ roʊˈdɒp sɪn)

n.
a protein complex that contains retinal and is used by halobacteria for photosynthesis instead of chlorophyll.
[1975–80]
References in periodicals archive ?
"Saturable absorption, wave mixing, and phase conjugation with bacteriorhodopsin." Optics Lett.
Similar to the case of the bacteriorhodopsin, RC also accomplishes a photocycle-accompanying tunable lifetimes and wavelength ranges of absorption and refractive index changes from sub-ps to s time scales [20, 69] (Figure 6).
Using this type of cryo-EM, we analyzed the structure of bacteriorhodopsin, which was analyzed for the first time by Henderson and Unwin, pioneers in electron crystallography, (17) together with the loop regions and lipid molecules at a resolution of 3.0 [Angstrom].
Bashford, "pK[alpha] calculations suggest storage of an excess proton in a hydrogen-bonded water network in bacteriorhodopsin," Journal of Molecular Biology, vol.
A good comparison of large-area, erasable holographic materials, such as Bacteriorhodopsin, Azo-dye, Electrothermoplastic, Amorphous Chalcogenide, Photorefractive polymers, and Liquid crystal systems by Peyghambarian's group can be found here [37].
Gerwert, "Bacteriorhodopsin's intramolecular proton-release pathway consists of a hydrogen-bonded network," Biochemistry, vol.
Microbial rhodopsins function as phototaxis receptors (sensory rhodopsin), light-driven proton or chloride ion transporters (bacteriorhodopsin and halorhodopsin) [2, 3, 5, 6, 8].
Their topics include templating photoreactions in solutions, supramolecular photochirogenesis, the photochromism of multicomponent diarylethene crystals, controlling photoreactions through non-covalent interactions within zeolite nanocages, and protein-controlled ultrafast photoisomerization in rhodopsin and bacteriorhodopsin.
In another innovative approach, artificially prepared vesicles known as liposomes were assembled on a quartz crystal microbalance via layer-by-layer growth using the membrane protein bacteriorhodopsin as a binding reagent.
For instance, light-activated excitation of rhodopsin (bacteriorhodopsin) molecules, involved in the hyperpolarization process of the cell membrane, can either generate nerve impulses, ATP synthesis, or regulate embryogenesis [1-5].
Characterization of proline-containing alpha-helix (helix F model of bacteriorhodopsin) by molecular dynamics studies.