Search results for "cooperativity"

showing 10 items of 78 documents

Influence of negative allosteric cooperativity in cation transport.

1992

Abstract The bis-macrocyclic ether5 seems to have a negative allosteric cooperativity and is able to transport double the amount of Na+ and K+ cations as monocyclic systems. This compound could be used as a simple model of the plasma membrane Na+−K+ ATPase which actively pumps Na+ out and K+ into the cell, respectively.

chemistry.chemical_classificationbiologyChemistryATPaseSodiumOrganic ChemistryAllosteric regulationInorganic chemistryIonophorechemistry.chemical_elementCooperativityBiochemistryCrystallographyMembraneDrug Discoverybiology.proteinCrown etherCation transportTetrahedron Letters
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Molecular and Functional Characterisation of Hemocyanin of the Giant African Millipede Archispirostreptus gigas

2013

SummaryIn contrast to other terrestrial arthropods where gaseous O2 that fuels aerobic metabolism diffuses to the tissues in tracheal tubes, and most other metazoans where O2 is transported to tissues by circulating respiratory proteins, the myriapods (millipedes and centipedes) strikingly have tracheal systems as well as circulating hemocyanin (Hc). In order to elucidate the evolutionary origin and biological significance of millipede Hc we report the molecular structure (subunit composition and amino acid sequence) of multimeric (36-mer) Hc from the forest-floor dwelling giant African millipede Archispirostreptus gigas and its allosteric oxygen binding properties under various physico-che…

Archispirostreptus gigasGlycosylationPhysiologymedicine.medical_treatmentProtein subunitAllosteric regulationMolecular Sequence DataCoenzymesBohr effectCooperativityAquatic ScienceBiologyModels Biologicalchemistry.chemical_compoundAllosteric RegulationmedicineAnimalsBody SizeMolecular BiologyPeptide sequenceArthropodsEcology Evolution Behavior and SystematicsPhylogenyHemocyaninBayes TheoremHydrogen-Ion Concentrationbiology.organism_classificationOxygenchemistryBiochemistryInsect ScienceAfricaHemocyaninsAnimal Science and ZoologyCalciumElectrophoresis Polyacrylamide GelProtein Binding
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Cover Picture: Achieving Strong Positive Cooperativity through Activating Weak Non‐Covalent Interactions (Angew. Chem. Int. Ed. 3/2018)

2018

chemistry.chemical_classificationchemistryStereochemistrySupramolecular chemistryCooperative bindingNon-covalent interactionsCover (algebra)CooperativityGeneral ChemistrySelf-assemblyHost–guest chemistryCatalysisAngewandte Chemie International Edition
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Molecular Mobility in Oriented and Unoriented Membranes Based on Poly[2-(Aziridin-1-yl)ethanol]

2021

Unoriented and oriented membranes based on dendronized polymers and copolymers obtained by chemical modification of poly[2-(aziridin-1-yl) ethanol] (PAZE) with the dendron 3,4,5-tris[4-(n-dodecan-1-yloxy)benzyloxy]benzoate were considered. DSC, XRD, CP-MAS NMR and DETA, contribute to characterize the tendency to crystallize, the molecular mobility of the benzyloxy substituent, the dendritic liquid crystalline group and the clearing transition. The orientation of the mesogenic chain somewhat hindered this molecular motion, especially in the full substituted PAZE. The fragility, free volume and thermal expansion coefficients of these membranes near the glass transition are related to the orie…

chemistry.chemical_classificationMaterials sciencePolymers and PlasticsMesogenSupramolecular chemistrySubstituentIonic bondingGeneral ChemistryPolymerQuímicaArticledielectric relaxation spectralcsh:QD241-441chemistry.chemical_compoundCrystallographyMembranepoly[2-(aziridin-1-yl)ethanol] (PAZE)chemistrylcsh:Organic chemistryDendrimerdendronic liquid crystal membranessegmental dynamicsmacromolecular cooperativityGlass transitionMaterialsPolymers
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Nested MWC model describes hydrolysis of GroEL without assuming negative cooperativity in binding

2002

Folding assistance and ATPase activity of GroEL are based on the existence of different conformations. In order to characterise these conformations, published data on steady state ATPase activity in the absence of GroES were reanalysed simultaneously in terms of the Nested MWC model. This model is a hierarchical extension of the symmetry-model of Monod et al. [J. Mol. Biol. 12 (1965) 88]. An unique set of GroEL specific parameters was obtained. This set was supported by comparison of predictions arising from this set of values with experimental data for hydrolysis of ATP in the presence of ADP and ATPgammaS, binding of ATPgammaS and ADP to GroEL in the absence of ATP, and binding of ATP as …

Adenosine TriphosphatasesModels Molecularchemistry.chemical_classificationChemistryHydrolysisBiophysicsCooperative bindingCooperativityChaperonin 60GroESBiochemistryGroELAnalytical ChemistryAdenosine DiphosphateFolding (chemistry)CrystallographyAdenosine TriphosphateATP hydrolysisCalibrationBiophysicsComputer SimulationNucleotideSteady state (chemistry)Molecular BiologyProtein BindingBiochimica et Biophysica Acta (BBA) - Proteins and Proteomics
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The Monod-Wyman-Changeux allosteric model accounts for the quaternary transition dynamics in wild type and a recombinant mutant human hemoglobin

2012

International audience; The acknowledged success of the Monod-Wyman-Changeux (MWC) allosteric model stems from its efficacy in accounting for the functional behavior of many complex proteins starting with hemoglobin (the paradigmatic case) and extending to channels and receptors. The kinetic aspects of the allosteric model, however, have been often neglected, with the exception of hemoglobin and a few other proteins where conformational relaxations can be triggered by a short and intense laser pulse, and monitored by time-resolved optical spectroscopy. Only recently the application of time-resolved wide-angle X-ray scattering (TR-WAXS), a direct structurally sensitive technique, unveiled th…

Models MolecularProtein ConformationcooperativityMESH: Catalytic DomainCooperativity01 natural sciencesMESH: Recombinant ProteinsHemoglobinsProtein structureMESH: Protein ConformationCatalytic Domainprotein structural dynamicsMESH: Allosteric Site0303 health sciencesMultidisciplinaryallosterybiologyMESH: KineticsChemistryBiological SciencesRecombinant Proteins[SDV.BBM.BP]Life Sciences [q-bio]/Biochemistry Molecular Biology/BiophysicsMESH: HemoglobinsAllosteric SiteMESH: Models MolecularAdultMESH: MutationStereochemistryKineticsAllosteric regulation010402 general chemistry03 medical and health sciencesprotein conformational changesflash photolysisallostery; cooperativity; flash photolysis; hemoglobin; protein conformational changes; protein structural dynamics; time-resolved wide angle x ray scattering; time-resolved x-ray scatteringHumans030304 developmental biologytime-resolved X-ray scattering; protein conformational changes; cooperativity; flash photolysisMESH: Humanstime-resolved X-ray scatteringWild typeActive sitetime-resolved wide angle x ray scatteringMESH: AdulthemoglobinSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)0104 chemical sciencesprotein conformational changeKineticsAllosteric enzymeMutationbiology.proteinHemoglobin
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Kinetic properties of hexameric tyrosinase from the crustacean Palinurus elephas.

2008

Tyrosinases catalyze hydroxylation of monophenols to o-diphenols and their subsequent oxidation to o-quinones, whereas catecholoxidases catalyze only the latter reaction. Both enzymes occur in all organisms and are Type 3 copper proteins that perform the first steps of melanin formation. In arthropods, they play an essential role in the sclerotization of the exoskeleton. Very few phenoloxidases are characterized structurally or kinetically and the existence of an actual tyrosinase activity has not been demonstrated in most cases. Here we present for the first time a complete kinetic characterization of a tyrosinase from a crustacean (Palinurus elephas) including the influence of inhibitors.…

StereochemistryCopper proteinTyrosinaseDopamineAllosteric regulationTyramineCooperativityBiologyBiochemistryBinding CompetitiveHydroxylationchemistry.chemical_compoundNon-competitive inhibitionAnimalsMimosinePhysical and Theoretical ChemistryEnzyme InhibitorsPalinuridaechemistry.chemical_classificationBinding SitesMolecular StructureMonophenol MonooxygenaseGeneral MedicinePhenylthioureaKineticsEnzymechemistryBiochemistryMimosineAllosteric SitePhotochemistry and photobiology
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Bis-cyclohexyl-crown-ethers as allosteric carriers

1992

Abstract Several bis-cyclohexyl-crown-ethers have been synthesized and used as carriers for alkaline cations. These compounds should all show negative allosteric cooperativity, but only 1 exhibits an odd cation transport behavior across the liquid organic membranes.

MembraneChemistryBiological modelingOrganic ChemistryDrug DiscoveryAllosteric regulationCrown (botany)Polymer chemistryIonophoreOrganic chemistryCooperativityBiochemistryCation transportTetrahedron
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Influence of the polymerization step alone on oxygen affinity and cooperativity during production of hyperpolymers from native hemoglobins with cross…

1994

The aim of this study was to find out how the polymerization per se changes oxygen affinity (P50) and cooperativity (n50) of various soluble huge hyperpolymers prepared from native hemoglobins by crosslinking. Increase of cooperativity would be expected considering natural hemoglobin networks. Those hyperpolymers with molecular weights of some 10(6) g/mol are candidates for artificial oxygen-carrying blood additives rather than volume substitutes. Human and bovine hemoglobin reacted with several crosslinkers (2,5-diisothiocyanatobenzenesulfonate (DIBS); 4,4'-diisothiocyanatostilbene-2, 2'-disulfonate (DIDS); 1,3-butadiene diepoxide (BUDE); glutaraldehyde (GDA)) in concentrated (case 1) and …

PolymersBiomedical EngineeringCooperativity44'-Diisothiocyanostilbene-22'-Disulfonic AcidIn Vitro TechniquesBlood substitutechemistry.chemical_compoundHemoglobinsBlood SubstitutesIsothiocyanatesPolymer chemistryOrganic chemistryAnimalsHumansMolecular massChemistryBenzenesulfonatesMolecular WeightOxygenSolutionsMonomerCross-Linking ReagentsPolymerizationDIDSGlutaralEpoxy CompoundsCattleGlutaraldehydeHemoglobinThiocyanatesBiotechnologyArtificial cells, blood substitutes, and immobilization biotechnology
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The interplay between cooperativity and diversity in model threshold ensembles

2014

The interplay between cooperativity and diversity is crucial for biological ensembles because single molecule experiments show a significant degree of heterogeneity and also for artificial nanostructures because of the high individual variability characteristic of nanoscale units. We study the cross-effects between cooperativity and diversity in model threshold ensembles composed of individually different units that show a cooperative behaviour. The units are modelled as statistical distributions of parameters (the individual threshold potentials here) characterized by central and width distribution values. The simulations show that the interplay between cooperativity and diversity results …

genetic structuresChemistrySystems biologySystems BiologyCell MembraneBiomedical EngineeringBiophysicsElectric ConductivityNanotechnologyCooperativityBioengineeringModels TheoreticalBiochemistryNanostructuresBiomaterialsProbability distributionComputer SimulationThreshold responseBiological systemResearch ArticlesBiotechnologyDiversity (business)
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