Search results for "binding"

showing 10 items of 3896 documents

Structural and Functional Analysis of the Antiparallel Strands in the Lumenal Loop of the Major Light-harvesting Chlorophyll a/b Complex of Photosyst…

2007

The light-harvesting chlorophyll a/b-binding protein of photosystem II (LHCIIb) fulfills multiple functions, such as light harvesting and energy dissipation under different illuminations. The crystal structure of LHCIIb at the near atomic resolution reveals an antiparallel strands structure in the lumenal loop between the transmembrane helices B/C. To study the structural and functional significances of this structure, three amino acids (Val-119, His-120, and Ser-123) in this region have been exchanged to Phe, Leu, and Gly, respectively, and the influence of the mutagenesis on the structure and function of LHCIIb has been investigated. The results are as follows. 1) Circular dichroism spect…

ChlorophyllModels MolecularCircular dichroismPhotosystem IIRecombinant Fusion ProteinsLight-Harvesting Protein ComplexesAntiparallel (biochemistry)BiochemistryFluorescencechemistry.chemical_compoundNeoxanthinSite-directed mutagenesisMolecular BiologyPlant ProteinsPhotobleachingChemistryChlorophyll ACircular DichroismPeasPhotosystem II Protein ComplexCell BiologyFluorescenceTransmembrane domainB vitaminsCrystallographyMutationMutagenesis Site-DirectedProtein BindingJournal of Biological Chemistry
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Amino acids in the second transmembrane helix of the Lhca4 subunit are important for formation of stable heterodimeric light-harvesting complex LHCI-…

2007

Photosynthetic light-harvesting complexes (LHCs) are assembled from apoproteins (Lhc proteins) and non-covalently attached pigments. Despite a considerable amino acid sequence identity, these proteins differ in their oligomerization behavior. To identify the amino acid residues determining the heterodimerization of Lhca1 and Lhca4 to form LHCI-730, we mutated the poorly conserved second transmembrane helix of the two subunits. Mutated genes were expressed in Escherichia coli and the resultant proteins were refolded in vitro and subsequently analyzed by gel electrophoresis. Replacement of the entire second helix in Lhca4 by the one of Lhca3 abolished heterodimerization, whereas it had no eff…

ChlorophyllModels MolecularMolecular Sequence DataLight-Harvesting Protein ComplexesBiologyProtein Structure SecondarySerineSolanum lycopersicumStructural BiologyChlorophyll bindingConsensus sequenceHistidineHomology modelingAmino Acid SequenceAmino AcidsProtein Structure QuaternaryMolecular BiologyPeptide sequenceHistidinePlant Proteinschemistry.chemical_classificationPhotosystem I Protein ComplexAmino acidTransmembrane domainProtein SubunitschemistryBiochemistryMutagenesisChlorophyll Binding ProteinsDimerizationSequence AlignmentJournal of molecular biology
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Expression of a higher plant light-harvesting chlorophyll a/b-binding protein in Synechocystis sp. PCC 6803

1999

A chimeric lhcb gene, coding for Lhcb, a higher plant chlorophyll a/b-binding light-harvesting complex of photosystem II (LHCII), was constructed using the Synechocystis sp. PCC 6803 psbA3 promoter and a modified lhcb gene from pea. This construct drives synthesis of full-length, mature Lhcb under the control of the strong psbA3 promoter that usually drives expression of the D1 protein of photosystem II. This chimeric gene was transformed into a photosystem I-less/chlL(-) Synechocystis sp. PCC 6803 strain that is unable to synthesize chlorophyll in darkness. In the resulting strain, a high level of lhcb transcript was detected and transcript accumulation was enhanced by addition of exogenou…

ChlorophyllPhotosystem IIRecombinant Fusion ProteinsPhotosynthetic Reaction Center Complex ProteinsPigment bindingMutantLight-Harvesting Protein ComplexesGene ExpressionChimeric geneBiologyCyanobacteriaBiochemistrychemistry.chemical_compoundTransformation GeneticIntegral membrane proteinChromatography High Pressure LiquidPlant ProteinsPhotosystemModels GeneticPhotosystem I Protein ComplexPhotosystem II Protein ComplexPigments BiologicalSpectrometry FluorescenceBiochemistrychemistryThylakoidChlorophyllRNAEuropean Journal of Biochemistry
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Water soluble chlorophyll binding protein of higher plants: A most suitable model system for basic analyses of pigment–pigment and pigment–protein in…

2011

Abstract This short review paper describes spectroscopic studies on pigment–pigment and pigment–protein interactions of chlorophyll (Chl) a and b bound to the recombinant protein of class IIa water soluble chlorophyll protein (WSCP) from cauliflower. Two Chls form a strongly excitonically coupled open sandwich dimer within the tetrameric protein matrix. In marked contrast to the mode of excitonic coupling of Chl and bacterio-Chl molecules in light harvesting complexes and reaction centers of all photosynthetic organisms, the unique structural pigment array in the Chl dimer of WSCP gives rise to an upper excitonic state with a large oscillator strength. This property opens the way for thorou…

ChlorophyllPhysiologyTetrameric proteinDimerLight-Harvesting Protein ComplexesTemperatureWatermacromolecular substancesPlant SciencePlantsPhotochemistryPhotosynthesisModels BiologicalLight-harvesting complexchemistry.chemical_compoundPigmentchemistryChlorophyllvisual_artvisual_art.visual_art_mediumChlorophyll bindingMoleculeAgronomy and Crop ScienceJournal of Plant Physiology
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IM30 triggers membrane fusion in cyanobacteria and chloroplasts

2015

The thylakoid membrane of chloroplasts and cyanobacteria is a unique internal membrane system harbouring the complexes of the photosynthetic electron transfer chain. Despite their apparent importance, little is known about the biogenesis and maintenance of thylakoid membranes. Although membrane fusion events are essential for the formation of thylakoid membranes, proteins involved in membrane fusion have yet to be identified in photosynthetic cells or organelles. Here we show that IM30, a conserved chloroplast and cyanobacterial protein of approximately 30 kDa binds as an oligomeric ring in a well-defined geometry specifically to membranes containing anionic lipids. Triggered by Mg2+, membr…

ChloroplastsGeneral Physics and AstronomyBiologyMembrane FusionThylakoidsGeneral Biochemistry Genetics and Molecular BiologyBacterial ProteinsCentrifugation Density GradientIntegral membrane proteinMultidisciplinaryGalactolipidsPeripheral membrane proteinSynechocystisLipid bilayer fusionfood and beveragesPhosphatidylglycerolsGeneral ChemistryTransmembrane proteinCell biologyChloroplastMembraneThylakoidLiposomesQuantasomeGlycolipidsProtein BindingNature Communications
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Evaluation of enantioselective binding of antihistamines to human serum albumin by ACE.

2007

The drug binding to plasma and tissue proteins is a fundamental factor in determining the overall pharmacological activity of a drug. HSA, together with alpha(1)-acid glycoprotein, are the most important plasma proteins, which act as drug carriers, with implications on the pharmacokinetic of drugs. Among plasma proteins, HSA possesses the highest enantioselectivity. In this paper, a new methodology for the study of enantiodifferentiation of chiral drugs with HSA is developed and applied to evaluate the possible enantioselective binding of four antihistamines: brompheniramine, chlorpheniramine, hydroxyzine and orphenadrine to HSA. This study includes the determination of affinity constants o…

ChlorpheniramineClinical BiochemistryPlasma protein bindingPharmacologyBiochemistryAnalytical ChemistryPharmacokineticsOrphenadrinemedicineOrphenadrineHumansSerum AlbuminDrug CarriersChromatographyBinding SitesChemistryBiological activityStereoisomerismBrompheniramineHuman serum albuminBrompheniraminebody regionsHydroxyzineembryonic structuresHistamine H1 AntagonistsEnantiomerDrug carriermedicine.drugProtein BindingElectrophoresis
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Displacement of phenprocoumon (Marcumar) from albumin by sulfonylurea compounds, suramin, and ioglycamic acid.

1972

The technique of Sephadex gel filtration was employed to characterize the effect of some sulfonylurea compounds, ioglycamic acid, and suramin on the binding of phenprocoumon to bovine serum albumin.

ChlorpropamideChlorpropamideSuraminTolbutamideSerum albuminSuraminIn Vitro TechniquesBenzoatesPhenprocoumonCoumarinsBenzyl CompoundsmedicineAnimalsBovine serum albuminPharmacologyChromatographyBinding SitesbiologyChemistryAlbuminAnticoagulantsDextransSerum Albumin BovineGeneral MedicineCarbutamideGlycolatesCarbutamideSulfonylurea CompoundsSephadexbiology.proteinChromatography GelIodobenzoatesCattlemedicine.drugProtein BindingNaunyn-Schmiedeberg's archives of pharmacology
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Down-regulation of transcription factors AP-1, Sp-1, and NF-kappa B precedes myocyte differentiation.

1996

Terminal differentiation of myocytes involves withdrawal from the cell cycle, induction of myogenin expression, and finally formation of myotubes. To study the factors that regulate the initial phase of muscle differentiation, we analyzed the binding activities of transcription factors AP-1, Sp-1, and NF-kappa B in L6, C2C12, and rhabdomyosarcoma BA-Han-1C cells. Temporal changes in transcription factor binding activities were compared to the activation of myogenin promoter-driven CAT reporter gene and the expression level of myogenin, a master gene of myogenic differentiation. We observed a prominent decrease in the nuclear binding activities of AP-1, Sp-1, and NF-kappa B already 12 to 24 …

Cholera ToxinSp1 Transcription FactorCellular differentiationBiophysicsDown-RegulationBiologyMuscle DevelopmentBiochemistryRetinoblastoma ProteinCell FusionMiceOkadaic AcidTumor Cells CulturedMyocyteAnimalsMuscle SkeletalMolecular BiologyTranscription factorMyogeninCell fusionMyogenesisNF-kappa BCell DifferentiationCell BiologyCell cyclemusculoskeletal systemMolecular biologyRatsUp-RegulationTranscription Factor AP-1MyogeninC2C12Protein BindingBiochemical and biophysical research communications
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Cholesterol reporter molecules.

2007

Cholesterol is a major constituent of the membranes in most eukaryotic cells where it fulfills multiple functions. Cholesterol regulates the physical state of the phospholipid bilayer, affects the activity of several membrane proteins, and is the precursor for steroid hormones and bile acids. Cholesterol plays a crucial role in the formation of membrane microdomains such as “lipid rafts” and caveolae. However, our current understanding on the membrane organization, intracellular distribution and trafficking of cholesterol is rather poor. This is mainly due to inherent difficulties to label and track this small lipid. In this review, we describe different approaches to detect cholesterol in …

Cholesterol oxidaseBacterial ToxinsBiophysicsBiologyBiochemistryFilipinchemistry.chemical_compoundHemolysin ProteinsMembrane MicrodomainsCaveolaeAnimalsHumansFilipinLipid bilayerMolecular BiologyLipid raftFluorescent DyesCholesterolCholesterol OxidaseCholesterol bindingCell BiologyCholesterolEukaryotic CellschemistryMembrane proteinBiochemistryMolecular Probeslipids (amino acids peptides and proteins)Bioscience reports
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Cholesterol–Protein Interaction: Methods and Cholesterol Reporter Molecules

2010

Cholesterol is a major constituent of the plasma membrane in eukaryotic cells. It regulates the physical state of the phospholipid bilayer and is crucially involved in the formation of membrane microdomains. Cholesterol also affects the activity of several membrane proteins, and is the precursor for steroid hormones and bile acids. Here, methods are described that are used to explore the binding and/or interaction of proteins to cholesterol. For this purpose, a variety of cholesterol probes bearing radio-, spin-, photoaffinity- or fluorescent labels are currently available. Examples of proven cholesterol binding molecules are polyene compounds, cholesterol-dependent cytolysins, enzymes acce…

Cholesterolmedicine.medical_treatmentCholesterol bindingSteroidProtein–protein interactionchemistry.chemical_compoundchemistryMembrane proteinBiochemistryMembrane fluiditymedicinelipids (amino acids peptides and proteins)Cholesterol 24-hydroxylaseLipid bilayer
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