Search results for "conformation"

showing 10 items of 1414 documents

Small-angle neutron scattering reveals an oxygen-dependent conformational change of the immunogen keyhole limpet hemocyanin type 1 (KLH1).

2001

The respiratory protein of the keyhole limpet, Megathura crenulata, the hemocyanin (KLH), commonly used as an immunogen, binds oxygen cooperatively, which implies the existence of different conformations. For the first time, two different conformations of KLH1 were detected upon oxygenation, a deoxy and an oxy state, using small-angle neutron scattering. Rearrangements in the quaternary structure of KLH1 were predicted from the different radii of gyration and the shifts of the minima and maxima in the scattering curves. Upon oxygenation, KLH1 becomes smaller and more compact. Model reconstruction of KLH1 indicates a hollow cylinder with two rings located close to both ends, which move sligh…

Conformational changeProtein Conformationmedicine.medical_treatmentBiophysicsNeutron scatteringMegathura crenulataBiophysical PhenomenamedicineAnimalsScattering RadiationProtein Structure QuaternaryNeutronsbiologyChemistryScatteringHemocyaninGeneral Medicinebiology.organism_classificationSmall-angle neutron scatteringRespiratory proteinOxygenCrystallographyMolluscaHemocyaninsbiology.proteinKeyhole limpet hemocyaninProtein BindingEuropean biophysics journal : EBJ
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Further Evidence that Papillomavirus Capsids Exist inTwo DistinctConformations

2003

ABSTRACT Cell surface heparan sulfate proteoglycans (HSPGs) serve as primary attachment receptors for human papillomaviruses (HPVs). To demonstrate that a biologically functional HPV-receptor interaction is restricted to a specific subset of HSPGs, we first explored the role of HSPG glucosaminoglycan side chain modifications. We demonstrate that HSPG O sulfation is essential for HPV binding and infection, whereas de-N-sulfated heparin interfered with VLP binding but not with HPV pseudoinfection. This points to differences in VLP-HSPG and pseudovirion-HSPG interactions. Interestingly, internalization kinetics of VLPs and pseudovirions, as measured by fluorescence-activated cell sorting analy…

Conformational changeProtein Conformationvirusesmedia_common.quotation_subjectImmunologyReplicationBiologyAntibodies ViralMicrobiologyEpitopeEpitopesMiceCapsidProtein structureNeutralization TestsVirologyChlorocebus aethiopsAnimalsHumansReceptorInternalizationPapillomaviridaemedia_commonCOS cellsVirionAntibodies MonoclonalCell sortingFlow CytometryMolecular biologyCell biologycarbohydrates (lipids)CapsidInsect ScienceCOS CellsReceptors VirusCapsid ProteinsHeparan Sulfate ProteoglycansJournal of Virology
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Molecular architecture of a toxin pore: a 15-residue sequence lines the transmembrane channel of staphylococcal alpha-toxin.

1996

Staphylococcus aureus alpha-toxin is a hydrophilic polypeptide of 293 amino acids that produces heptameric transmembrane pores. During assembly, the formation of a pre-pore precedes membrane permeabilization; the latter is linked to a conformational change in the oligomer. Here, 41 single-cysteine replacement toxin mutants were thiol-specifically labelled with the polarity-sensitive fluorescent probe acrylodan. After oligomerization on membranes, only the mutants with acrylodan attached to residues in the sequence 118-140 exhibited a marked blue shift in the fluorescence emission maximum, indicative of movement of the fluorophore to a hydrophobic environment. Within this region, two functio…

Conformational changeStaphylococcus aureusProtein ConformationMembrane lipidsBacterial ToxinsMolecular Sequence DataBiologyGeneral Biochemistry Genetics and Molecular BiologyCell membraneHemolysin ProteinsProtein structure2-NaphthylaminemedicinePoint MutationAmino Acid SequenceCysteineMolecular BiologyPeptide sequenceFluorescent Dyeschemistry.chemical_classificationBinding SitesGeneral Immunology and MicrobiologyMolecular StructureGeneral NeuroscienceCell MembraneTransmembrane proteinAmino acidmedicine.anatomical_structureMembraneSpectrometry FluorescenceBiochemistrychemistryLiposomesBiophysicsMutagenesis Site-DirectedResearch ArticleThe EMBO journal
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Antigen recognition by T cells: a strong sense of structure

2001

Conformational changeStructural organizationStructural biologyImmunologyT-cell receptorSense (molecular biology)ImmunologyImmunology and AllergyComputational biologyAntigen recognitionBiologyTrends in Immunology
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Protofibril formation of amyloid beta-protein at low pH via a non-cooperative elongation mechanism.

2005

Deposition of the amyloid beta-protein (Abeta) in senile or diffuse plaques is a distinctive feature of Alzheimer's disease. The role of Abeta aggregates in the etiology of the disease is still controversial. The formation of linear aggregates, known as amyloid fibrils, has been proposed as the onset and the cause of pathological deposition. Yet, recent findings suggest that a more crucial role is played by prefibrillar oligomeric assemblies of Abeta that are highly toxic in the extracellular environment. In the present work, the mechanism of protofibril formation is studied at pH 3.1, starting from a solution of oligomeric precursors. By combining static light scattering and photon correla…

Conformational changeTime FactorsAmyloidLightNucleationBiophysicsBiochemistryBiophysical PhenomenaDiffusionDynamic light scatteringAlzheimer DiseaseExtracellularHumansScattering RadiationStatic light scatteringMolecular BiologyCoalescence (physics)PhotonsAmyloid beta-PeptidesModels StatisticalDose-Response Relationship DrugChemistryTemperatureCell BiologyHydrogen-Ion ConcentrationModels TheoreticalCrystallographyKineticsSpectrophotometryBiophysicsThermodynamicsElongationPeptidesProtein BindingThe Journal of biological chemistry
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Human Inducible Hsp70: Structures, Dynamics, and Interdomain Communication from All-Atom Molecular Dynamics Simulations

2015

The 70 kDa human heat shock protein is a major molecular chaperone involved in de novo folding of proteins in vivo and refolding of proteins under stress conditions. Hsp70 is related to several "misfolding diseases" and other major pathologies, such as cancer, and is a target for new therapies. Hsp70 is comprised of two main domains: an N-terminal nucleotide binding domain (NBD) and a C-terminal substrate protein binding domain (SBD). The chaperone function of Hsp70 is based on an allosteric mechanism. Binding of ATP in NBD decreases the affinity of the substrate for SBD, and hydrolysis of ATP is promoted by binding of polypeptide segments in the SBD. No complete structure of human Hsp70 is…

Conformational changebiologySaccharomyces cerevisiaeAllosteric regulationPlasma protein bindingbiology.organism_classificationComputer Science ApplicationsMolecular dynamicsBiochemistryCyclic nucleotide-binding domainATP hydrolysisChaperone (protein)biology.proteinBiophysicsPhysical and Theoretical ChemistryJournal of Chemical Theory and Computation
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Evidence for Conformational Mechanism on the Binding of TgMIC4 with β-Galactose-Containing Carbohydrate Ligand

2015

A deeper understanding of the role of sialic/desialylated groups during TgMIC4-glycoproteins interactions has importance to better clarify the odd process of host cell invasion by members of the apicomplexan phylum. Within this context, we evaluated the interaction established by recombinant TgMIC4 (the whole molecule) with sialylated (bovine fetuin) and desialylated (asialofetuin) glycoproteins by using functionalized quartz crystal microbalance with dissipation monitoring (QCM-D). A suitable receptive surface containing recombinant TgMIC4 for monitoring β-galactose-containing carbohydrate ligand (limit of quantification ∼ 40 μM) was designed and used as biomolecular recognition platform t…

Conformational changemedia_common.quotation_subjectCarbohydratesMolecular ConformationProtozoan ProteinsContext (language use)Plasma protein bindingLigandsElectrochemistryGeneral Materials ScienceInternalizationSpectroscopymedia_commonchemistry.chemical_classificationChemistryLigandLECTINASGalactoseSurfaces and InterfacesCondensed Matter PhysicsFetuinBiochemistryQuartz Crystal Microbalance TechniquesAdsorptionTarget proteinGlycoproteinToxoplasmaProtein BindingLangmuir
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Impact of Pulsed Electric Fields on Enzymes

2017

International audience; Pulsed electric field (PEF) processing has emerged as a promising technology in the development of tailor-made processes to effectively control the enzyme activity. It has been proven as an effective technique for the preservation of food products as it can result in substantial inactivation of most undesirable enzymes. When compared to microbial inactivation, however, large specific energy inputs are required to inactivate enzymes. The existing evidence suggests that PEF can also stimulate the activity of beneficial enzymes at low intense treatments. The PEF affects enzyme activity by changing mainly the secondary (α-helix, β-sheets, etc.), tertiary (spatial conform…

Conformational changes0301 basic medicineProteasesFood processing[SDV.BIO]Life Sciences [q-bio]/Biotechnology[SDV]Life Sciences [q-bio]010402 general chemistry01 natural sciencesPolyphenol oxidase03 medical and health sciences[SPI.GPROC]Engineering Sciences [physics]/Chemical and Process EngineeringEnzyme activityLipasePulsed electric fieldchemistry.chemical_classificationbiologyChemistryEnzyme structureEnzyme assayEnzymesrespiratory tract diseases0104 chemical sciences030104 developmental biologyEnzymeBiochemistrybiology.proteinAlkaline phosphatase[SDV.AEN]Life Sciences [q-bio]/Food and NutritionPeroxidase
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Über blei-haltige Heterocyclen

1990

Abstract Crystal structures of alternating six-membered rings [Ph2PbS]3-P21/c and [Ph2SnS]3-P21/n have been determined by X-ray methods. Both heterocycles exhibit a C2-symmetric twisted boat conformation with tetrahedral coordination of the metal atoms [dPbS 2.491 A (dSnS 2.401 A, dPbC 2.19 A (dSnC 2.129 A)]. No additional intermolecular contacts have been found. A ring-segment exchange reaction in solution has been observed by NMR. In the resulting equilibrium new cyclic compounds containing both tin and lead atoms with coupling constants 2J(207PbS119Sn) 226 Hz have been detected. FD-mass spectra indicate formation of dimeric molecular units.

Coupling constantChemistryStereochemistryOrganic ChemistryCyclohexane conformationIntermolecular forcechemistry.chemical_elementCrystal structureBiochemistrySpectral lineInorganic ChemistryMetalCrystallographyvisual_artMaterials Chemistryvisual_art.visual_art_mediumPhysical and Theoretical ChemistryTinJournal of Organometallic Chemistry
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A DFT study of the Karplus-type dependence of vicinal 3J(Sn-C-X- C), X=N,O,S, in organotin(iv) compounds: Application to conformationally flexible sy…

2010

ZORA relativistic and non-relativistic DFT protocols have been used to investigate vicinal coupling constants, (3)J(Sn-C-X-C), in several organotin(iv) compounds, with particular emphasis on cyclic alpha-aminoorganostannanes. The dependence of the coupling constant on the heteroatom X (X = N,O,S) in the coupling path, and, for X = N, its substituents, has been studied in detail. The electron-withdrawing strength of the N-substituents has been found to strongly affect the magnitude and shape of the Karplus-type curve. The results obtained for the simple model systems, having no or little conformational flexibility, have helped in rationalizing the data concerning real flexible cyclic systems…

Coupling constantCouplingeducation.field_of_study119Tin NMR vicinal coupling constants DFTChemistryOrganic ChemistryHeteroatomPopulationType (model theory)BiochemistryComputational chemistryPhysical and Theoretical ChemistryeducationConformational isomerismVicinal
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