Search results for "Cooperativity"

showing 10 items of 78 documents

Cooperative Transition in the Conformation of 24-Mer Tarantula Hemocyanin upon Oxygen Binding

2005

Hemocyanins are large respiratory proteins of arthropods and mollusks, which bind oxygen with very high cooperativity. Here, we investigated the relationship between oxygen binding and structural changes of the 24-mer tarantula hemocyanin. Oxygen binding of the hemocyanin was detected following the fluorescence intensity of the intrinsic tryptophans. Under the same conditions, structural changes were monitored by the non-covalently bound fluorescence probe Prodan (6-propionyl-2-(dimethylamino)-naphthalene), which is very sensitive to its surroundings. Upon oxygen binding of the hemocyanin a red shift of 5 nm in the emission maximum of the label was observed. A comparison of oxygen binding c…

Macromolecular SubstancesProtein ConformationPartial Pressuremedicine.medical_treatmentAllosteric regulationMolecular ConformationAnalytical chemistrychemistry.chemical_elementchemical and pharmacologic phenomenaCooperativitycomplex mixturesBiochemistryOxygenProtein structure2-NaphthylaminemedicineAnimalsBinding siteMolecular BiologyBinding SitesChemistryTryptophanSpidersHemocyaninCell BiologyFluorescenceOxygenSpectrometry FluorescenceMicroscopy FluorescenceModels ChemicalSpectrophotometryHemocyaninsBiophysicsAllosteric SiteOxygen bindingProtein BindingJournal of Biological Chemistry
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8-Azido-adenosine 5'-triphosphate as a Photoaffinity Label for Bacterial F1 ATPase

1978

1. 8-Azido-adenosine 5'-triphosphate (n83ATP) is a suitable photoaffinity label for F1 ATPase from Micrococcus luteus. The nucleotide is a substrate in the presence of bivalent cations and inhibits the enzyme irreversibly upon irradiation with ultraviolet light above 300 nm. 2. More than 80% of the label is covalently bound to the beta subunits in the presence of bivalent cations. Labeling and inactivation is decreased by protection with ADP, ATP or adenyl-5'-yl imidodiphosphate. To a much smaller degree the alpha subunits also become labeled. 3. n83AMP does not specifically bind to the beta subunits upon irradiation. Like n83ATP and n83ADP, it also labels the alpha subunits to a small exte…

Macromolecular SubstancesUltraviolet RaysATPaseAffinity labelCooperativityBiochemistryMicrococcuschemistry.chemical_compoundAdenosine TriphosphateAdenine nucleotideUltraviolet lightMagnesiumNucleotideEdetic AcidAdenosine Triphosphataseschemistry.chemical_classificationPhotolysisbiologyAdenine NucleotidesChemistryAffinity LabelsBiochemistrybiology.proteinCalciumAdenosine triphosphateATP synthase alpha/beta subunitsEuropean Journal of Biochemistry
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Identification, structure, and properties of hemocyanins from Diplopod myriapoda.

1999

Hemocyanins are copper-containing, respiratory proteins that occur in the hemolymph of many arthropod species. Here we report for the first time the presence of hemocyanins in the diplopod Myriapoda, demonstrating that these proteins are more widespread among the Arthropoda than previously thought. The hemocyanin of Spirostreptus sp. (Diplopoda: Spirostreptidae) is composed of two immunologically distinct subunits in the 75-kDa range that are most likely arranged in a 36-mer (6 x 6) native molecule. It has a high oxygen affinity (P(50) = 4.7 torr) but low cooperativity (h = 1.3 +/- 0.2). Spirostreptus hemocyanin is structurally similar to the single known hemocyanin from the myriapod taxon,…

MaleProtein Conformationmedicine.medical_treatmentBlotting WesternMyriapodachemical and pharmacologic phenomenaCooperativityCross Reactionscomplex mixturesBiochemistryEpitopesHemolymphmedicineAnimalsMolecular BiologyArthropodsbiologyhemic and immune systemsHemocyaninCell BiologyAnatomybiology.organism_classificationSpirostreptusOxygenBiochemistrySpectrophotometryHemocyaninsElectrophoresis Polyacrylamide GelFemaleArthropodSpirostreptidaeScutigera coleoptrataProtein BindingThe Journal of biological chemistry
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Identification and quantification of a new family of peptide endocannabinoids (Pepcans) showing negative allosteric modulation at CB1 receptors.

2012

The α-hemoglobin-derived dodecapeptide RVD-hemopressin (RVDPVNFKLLSH) has been proposed to be an endogenous agonist for the cannabinoid receptor type 1 (CB(1)). To study this peptide, we have raised mAbs against its C-terminal part. Using an immunoaffinity mass spectrometry approach, a whole family of N-terminally extended peptides in addition to RVD-Hpα were identified in rodent brain extracts and human and mouse plasma. We designated these peptides Pepcan-12 (RVDPVNFKLLSH) to Pepcan-23 (SALSDLHAHKLRVDPVNFKLLSH), referring to peptide length. The most abundant Pepcans found in the brain were tested for CB(1) receptor binding. In the classical radioligand displacement assay, Pepcan-12 was th…

MaleSus scrofaPeptideCooperativityBiochemistrychemistry.chemical_compoundAntibodies Monoclonal Murine-DerivedHemoglobinsMice0302 clinical medicineReceptor Cannabinoid CB1NeurobiologyTandem Mass SpectrometryCricetinaeRadioligandReceptorchemistry.chemical_classification0303 health sciencesMice Inbred NZBmusculoskeletal neural and ocular physiologyfood and beveragesBrainLigand (biochemistry)humanitiesProtein TransportBiochemistrylipids (amino acids peptides and proteins)FemaleEndogenous agonistProtein BindingSignal TransductionAllosteric regulationMolecular Sequence DataHL-60 CellsCHO CellsBiologyBinding Competitive03 medical and health sciencesAllosteric RegulationCannabinoid Receptor ModulatorsAnimalsHumansAmino Acid SequenceMolecular Biology030304 developmental biologyCell BiologyCyclohexanolsHemopressinPeptide FragmentsRatsMice Inbred C57BLchemistrynervous system030217 neurology & neurosurgeryEpitope MappingThe Journal of biological chemistry
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Cooperativity Scaling and Free Volume in Plasticized Polylactide

2019

The authors would like to thank the region Haute Normandie for their financial support and the acquisition of the Broadband Dielectric Spectrometer. R.G. acknowledges U.S. National Science Foundation (Grant no. DMR-1725188) for the acquisition of PAL spectrometer. The experimental evidence of the increase of activation energy associated with the super Arrhenius behavior governing amorphous polylactide by free volume variations has been obtained through a combination of calorimetric, dielectric, and positron annihilation lifetime measurements. The amount of free volume in polylactide was controlled by the amount of acetyltributylcitrate plasticizer in the composition. Plasticization is shown…

Materials scienceMatériaux [Sciences de l'ingénieur]Polymers and Plasticsgenetic structuresThermodynamicsCooperativity02 engineering and technologyActivation energyDielectric010402 general chemistry01 natural sciences[SPI.MAT]Engineering Sciences [physics]/MaterialsInorganic ChemistryFragilityBiopolymersmiscible polymer blendsMaterials ChemistryActivation energycharacteristic length[PHYS]Physics [physics]Drop (liquid)Organic polymersOrganic Chemistry021001 nanoscience & nanotechnology0104 chemical sciencesAmorphous solidfragilty[CHIM.POLY]Chemical Sciences/PolymersVolume (thermodynamics)positron-annihilationtemperature-dependence[PHYS.COND.CM-MS]Physics [physics]/Condensed Matter [cond-mat]/Materials Science [cond-mat.mtrl-sci]0210 nano-technologyGlass transitionPlastics[PHYS.COND.CM-SCM]Physics [physics]/Condensed Matter [cond-mat]/Soft Condensed Matter [cond-mat.soft]dynamic heterogeneity
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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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Hemocyanin from E. californicum encapsulated in silica gels: oxygen binding and conformational states.

2007

Cooperativity depends on the existence of equilibria among functionally distinct conformational states that are affected by homo and heterotropic effectors. In order to isolate the quaternary conformations of hemocyanin from E. californicum, the 24-meric giant protein was encapsulated in wet, nanoporous silica gels, either in the absence or presence of oxygen. The deoxy- and oxy-hemocyanin gels exhibit a p50 for oxygen of 11 and 2.5 torr, respectively, values in close agreement with those for hemocyanin in solution. The observed Hill coefficients are lower than unity, indicating a conformational heterogeneity within each locked conformational state, a finding in agreement with the assumptio…

Models MolecularAbsorption spectroscopyProtein Conformationmedicine.medical_treatmentchemistry.chemical_elementCooperativityBiologyOxygenGeneticsmedicineAnimalsNanoporousHemocyaninSpidersGeneral MedicineSilicon DioxideOxygenSolutionsCrystallographyKineticsBiochemistrychemistrySpectrophotometryHemocyaninsHemoglobinGelsOxygen bindingAlgorithmsProtein BindingGene
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All hierarchical levels are involved in conformational transitions of the 4×6-meric tarantula hemocyanin upon oxygenation

2002

The respiratory protein of the tarantula Eurypelma californicum is a 4 x 6-meric hemocyanin that binds oxygen with high cooperativity. This requires the existence of different conformations which have been confirmed by small angle X-ray scattering (SAXS). Here we present reconstructed 3D-models of the oxy- and deoxy-forms of tarantula hemocyanins, as obtained by fitting small angle X-rays scattering curves on the basis of known X-ray structures and electron microscopy of related hemocyanins. For the first time, the involvement of movements at all levels of the quaternary structure was confirmed for an arthropod hemocyanin upon oxygenation. The two identical 2 x 6-meric half-molecules of the…

Models MolecularMacromolecular SubstancesProtein Conformationmedicine.medical_treatmentAllosteric regulationBiophysicsCooperativityRandom hexamerBiochemistryOligomerAnalytical Chemistrychemistry.chemical_compoundmedicineAnimalsMolecular BiologySmall-angle X-ray scatteringSpidersHemocyaninOxygenRespiratory proteinCrystallographychemistryHemocyaninsProtein quaternary structureOxidation-ReductionProtein 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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Crystallization and Preliminary Analysis of Crystals of the 24-Meric Hemocyanin of the Emperor Scorpion (Pandinus imperator)

2011

Hemocyanins are giant oxygen transport proteins found in the hemolymph of several invertebrate phyla. They constitute giant multimeric molecules whose size range up to that of cell organelles such as ribosomes or even small viruses. Oxygen is reversibly bound by hemocyanins at binuclear copper centers. Subunit interactions within the multisubunit hemocyanin complex lead to diverse allosteric effects such as the highest cooperativity for oxygen binding found in nature. Crystal structures of a native hemocyanin oligomer larger than a hexameric substructure have not been published until now. We report for the first time growth and preliminary analysis of crystals of the 24-meric hemocyanin (M(…

Models MolecularSciencemedicine.medical_treatmentProtein subunitBiophysicsElectronschemical and pharmacologic phenomenaCooperativityBiologyCrystallography X-RayBiochemistrycomplex mixtures570 Life sciencesArthropod ProteinsScorpionsPandinusHemolymphMacromolecular Structure AnalysismedicineAnimalsMolecular replacementProtein Structure QuaternaryBiologyMultidisciplinaryQROxygen transportProteinsComputational BiologyHemocyaninAnatomybiology.organism_classificationCrystallographyHemocyaninsMedicineProtein MultimerizationCrystallizationOxygen binding570 BiowissenschaftenResearch ArticlePLoS ONE
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