Search results for "Chromoprotein"

showing 3 items of 3 documents

Partial purification and initial characterization of phytochrome from the mossAtrichum undulatum P. Beauv. grown in the light.

1988

The extraction and partial purification of phytochrome from light-grownAtrichum undulatum P. Beauv., a chlorophyllous moss, is described. Polyethyleneimine and salt fractionation followed by hydroxyapatite and Affi-gel-blue chromatography were used to separate phytochrome from chlorophyll, and to purify the pigment. All steps were performed in the presence of Triton X-100 which improved the yield by a factor of about three. The protein has a molecular weight some-what larger than that ofAvena phytochrome (124 kDa), as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and immunoblot analysis. It cross-reacts with a monoclonal antibody against phytochrome from etiolated …

Gel electrophoresisfood.ingredientbiologyPhytochromefood and beveragesPlant Sciencechemistry.chemical_compoundPigmentAvenafoodchemistryBiochemistryPolyclonal antibodiesChromoproteinChlorophyllvisual_artEtiolationGeneticsbiology.proteinvisual_art.visual_art_mediumPlanta
researchProduct

Probing a Polar Cluster in the Retinal Binding Pocket of Bacteriorhodopsin by a Chemical Design Approach

2012

Bacteriorhodopsin has a polar cluster of amino acids surrounding the retinal molecule, which is responsible for light harvesting to fuel proton pumping. From our previous studies, we have shown that threonine 90 is the pivotal amino acid in this polar cluster, both functionally and structurally. In an attempt to perform a phenotype rescue, we have chemically designed a retinal analogue molecule to compensate the drastic effects of the T90A mutation in bacteriorhodopsin. This analogue substitutes the methyl group at position C(13) of the retinal hydrocarbon chain by and ethyl group (20-methyl retinal). We have analyzed the effect of reconstituting the wild-type and the T90A mutant apoprotein…

Halobacterium salinarumModels MolecularProtein FoldingProtein Denaturation01 natural sciencesBiotecnologiaBiochemistryBiophysics Simulationschemistry.chemical_compoundSensory RhodopsinsHalobacterium salinarum0303 health sciencesMultidisciplinarybiologyProtein StabilityQRTemperatureUltraviolet-visible spectroscopyThermal stabilityBacterial BiochemistryChemistryBiochemistryBacteriorhodopsinsRetinaldehydeMedicineProtonsResearch ArticleSteric effectsHydrogen bondingBioquímicaProtein StructureScienceRetinal bindingBiophysics010402 general chemistryMicrobiologyPhosphates03 medical and health sciencesBiology030304 developmental biologyAspartic AcidBinding SitesAdaptation OcularOrganic ChemistryOrganic SynthesisProteinsChromoproteinsRetinalBacteriorhodopsinBacteriologyBiological TransportChromophorebiology.organism_classification0104 chemical sciencesTransmembrane ProteinschemistryRetinaldehydeBiophysicsbiology.proteinMutant ProteinsPLoS ONE
researchProduct

Light-driven proton transport of bacteriorhodopsin incorporated into long-term stable liposomes of a polymerizable sulfolipid

1983

Abstract The chromoprotein bacteriorhodopsin from Halobacterium halobium has been incorporated into liposomes made of a fully synthetic, polymerizable lipid. Bacteriorhodopsin is found to be active in these polymer liposomes. The advantage in the use of such polymer systems concerning long-term stability in comparison with liposomes made of natural lipid is demonstrated.

SulfolipidBiophysicsBacteriorhodopsinHalobacterium halobiumBiochemistrychemistry.chemical_compoundStructural BiologyChromoproteinProton transportGeneticsOrganic chemistryLight-driven proton pumpLong-term stabilityMolecular Biologychemistry.chemical_classificationLiposomebiologyBacteriorhodopsinCell BiologyPolymerLiposomechemistrybiological sciencesbiology.proteinLight drivenBiophysicsPolymerizable synthetic lipidFEBS Letters
researchProduct