Search results for "Interactions"

showing 10 items of 1963 documents

Decoding the Folding of Burkholderia glumae Lipase: Folding Intermediates En Route to Kinetic Stability

2012

The lipase produced by Burkholderia glumae folds spontaneously into an inactive near-native state and requires a periplasmic chaperone to reach its final active and secretion-competent fold. The B. glumae lipase-specific foldase (Lif) is classified as a member of the steric-chaperone family of which the propeptides of alpha-lytic protease and subtilisin are the best known representatives. Steric chaperones play a key role in conferring kinetic stability to proteins. However, until present there was no solid experimental evidence that Lif-dependent lipases are kinetically trapped enzymes. By combining thermal denaturation studies with proteolytic resistance experiments and the description of…

Macromolecular AssembliesProtein StructureProtein FoldingBurkholderiaProtein ConformationStereochemistryBiophysicslcsh:MedicineBiochemistryProtein Chemistrybacterial lipasemolten globuleBacterial ProteinsNative stateBurkholderia glumaeLipaseProtein Interactionslcsh:ScienceBiologyMultidisciplinarybiologylipase-specific foldasePhysicslcsh:RSubtilisinProteinsLipasebiology.organism_classificationMolten globuleEnzymesChaperone ProteinsKineticsBiochemistryChaperone (protein)Enzyme StructureProteolysisFoldasebiology.proteinlcsh:Qsteric chaperoneProtein foldingnear-native folding intermediateResearch ArticleMolecular Chaperones
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Acetylcholine-binding protein in the hemolymph of the planorbid snail Biomphalaria glabrata is a pentagonal dodecahedron (60 subunits).

2012

Nicotinic acetylcholine receptors (nAChR) play important neurophysiological roles and are of considerable medical relevance. They have been studied extensively, greatly facilitated by the gastropod acetylcholine-binding proteins (AChBP) which represent soluble structural and functional homologues of the ligand-binding domain of nAChR. All these proteins are ring-like pentamers. Here we report that AChBP exists in the hemolymph of the planorbid snail Biomphalaria glabrata (vector of the schistosomiasis parasite) as a regular pentagonal dodecahedron, 22 nm in diameter (12 pentamers, 60 active sites). We sequenced and recombinantly expressed two ∼25 kDa polypeptides (BgAChBP1 and BgAChBP2) wit…

Macromolecular AssembliesProtein StructureProtein FoldingScienceBiophysicsBiochemistryProtein ChemistryHomology (biology)Ion ChannelsProtein Structure Secondarylaw.inventionDodecahedronAcetylcholine bindinglawHemolymphHemolymphMacromolecular Structure AnalysisBiomphalaria glabrataAnimal PhysiologyAnimalsBiomacromolecule-Ligand InteractionsBiologyAcetylcholine receptorMultidisciplinaryHemoproteinsbiologyBiomphalariaQRActive siteProteinsComputational BiologyAnatomybiology.organism_classificationRecombinant ProteinsAcetylcholineProtein Structure TertiaryBiochemistryAcetylcholine Receptorsbiology.proteinRecombinant DNAMedicineCarrier ProteinsZoologyResearch ArticlePLoS ONE
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Unlocked Concanavalin A Forms Amyloid-like Fibrils from Coagulation of Long-lived "Crinkled'' Intermediates

2013

Understanding the early events during amyloid aggregation processes is crucial to single out the involved molecular mechanisms and for designing ad hoc strategies to prevent and reverse amyloidogenic disorders. Here, we show that, in conditions in which the protein is positively charged and its conformational flexibility is enhanced, Concanavalin A leads to fibril formation via a non-conventional aggregation pathway. Using a combination of light scattering, circular dichroism, small angle X-ray scattering, intrinsic (Tryptophan) and extrinsic (ANS) fluorescence and confocal and 2-photon fluorescence microscopy we characterize the aggregation process as a function of the temperature. We high…

Macromolecular AssembliesProteomicsCircular dichroismProtein StructureAmyloidProtein FoldingScienceMedical BiotechnologyBiophysics02 engineering and technologyFibrilBiochemistryProtein Chemistry03 medical and health sciencesProtein structureMedicinsk bioteknologiFluorescence microscopeNative stateConcanavalin ACoagulation (water treatment)Protein InteractionsBiology030304 developmental biology0303 health sciencesprotein aggregation amyloid concanavalin A intermediates spectroscopy advanced fluorescence microscopyMultidisciplinaryChemical PhysicsChemistryPhysicsCircular DichroismQRProteins021001 nanoscience & nanotechnologyProtein Structure TertiaryLuminescent ProteinsBiochemistryBiophysicsMedicineProtein folding0210 nano-technologyHydrophobic and Hydrophilic InteractionsFunction (biology)Research Article
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Aminopropyltransferases involved in polyamine biosynthesis localize preferentially in the nucleus of plant cells

2012

Plant aminopropyltransferases consist of a group of enzymes that transfer aminopropyl groups derived from decarboxylated S-adenosyl-methionine (dcAdoMet or dcSAM) to propylamine acceptors to produce polyamines, ubiquitous metabolites with positive charge at physiological pH. Spermidine synthase (SPDS) uses putrescine as amino acceptor to form spermidine, whereas spermine synthase (SPMS) and thermospermine synthase (TSPMS) use spermidine as acceptor to synthesize the isomers spermine and thermospermine respectively. In previous work it was shown that both SPDS1 and SPDS2 can physically interact with SPMS although no data concerning the subcellular localization was reported. Here we study the…

Macromolecular AssembliesProteomicsS-AdenosylmethioninePlant anatomyImmunohistoquímicaArabidopsislcsh:MedicineSecondary MetabolismSpermineExpressionPlant ScienceSpermidine synthaseBiochemistrychemistry.chemical_compoundBimolecular fluorescence complementationCytosolMolecular Cell BiologyPolyaminesPlant Genomicslcsh:SciencePlant Growth and DevelopmentMultidisciplinarybiologyPlant BiochemistryArabidopsis-ThalianaGenomicsImmunohistochemistryMetabolismeFunctional GenomicsBiochemistrySpermine synthasePlant proteinPlant PhysiologyMechanismResearch ArticleHistologyAcyltransferasePlant Cell BiologyActive Transport Cell NucleusSpermidine SynthaseBimolecular fluorescence complementationProtein InteractionsBiologyCell NucleusCrystal-Structurelcsh:RHistologiaBotanyProtein interactionsSubcellular localizationAnatomia vegetalExpressió gènicaMolecular WeightSpermidineMetabolismchemistryDecarboxylasebiology.proteinPutrescineBotànicalcsh:QGene expressionSpermidine synthase
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Construction of Chimeric Dual-Chain Avidin by Tandem Fusion of the Related Avidins

2011

BackgroundAvidin is a chicken egg-white protein with high affinity to vitamin H, also known as D-biotin. Many applications in life science research are based on this strong interaction. Avidin is a homotetrameric protein, which promotes its modification to symmetrical entities. Dual-chain avidin, a genetically engineered avidin form, has two circularly permuted chicken avidin monomers that are tandem-fused into one polypeptide chain. This form of avidin enables independent modification of the two domains, including the two biotin-binding pockets; however, decreased yields in protein production, compared to wt avidin, and complicated genetic manipulation of two highly similar DNA sequences i…

Macromolecular Assemblieslcsh:MedicineBiosensing TechniquesPolymerase Chain ReactionBiochemistryProtein Structure Secondarychemistry.chemical_compoundProtein structureBiotinMacromolecular Structure AnalysisProtein biosynthesisBiomacromolecule-Ligand InteractionsSurface plasmon resonancelcsh:Science0303 health sciencesMultidisciplinarybiologyrespiratory systemRecombinant ProteinsBiochemistryBiotinylationChromatography GelBiophysic Al SimulationsResearch ArticleProtein StructureStructural similarityRecombinant Fusion Proteins030303 biophysicsBiophysicsBiotinMolecular Dynamics SimulationBiokemia solu- ja molekyylibiologia - Biochemistry cell and molecular biology03 medical and health sciencesstomatognathic systemDefense ProteinsEscherichia coliAnimalsGene familyProtein InteractionsBiology030304 developmental biologylcsh:RProteinsComputational BiologySurface Plasmon ResonanceAvidinchemistrySmall MoleculesFermentationbiology.proteinlcsh:QChickensAvidinPLoS ONE
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1D antiferromagnetism in spin‐alternating bimetallic chains

1990

The magnetic and thermal properties of the ordered bimetallic chain CoNi(EDTA)⋅6H2O in the very low‐temperature range are reported. The magnetic behavior does not exhibit the characteristic features of 1D ferrimagnets, but a continuous decrease of χmT towards zero at absolute zero. This 1D antiferromagnetic behavior results from an accidental compensation between the moments located at the two sublattices. This behavior, as well as the specific‐heat results, are modeled on the basis of an Ising‐exchange model that considers both alternating spins and Landé factors, and a zero‐field splitting on the Ni site. Eugenio.Coronado@uv.es ; Fernando.Sapina@uv.es

Magnetic PropertiesEdtaExchange InteractionsGeneral Physics and AstronomyNickel CompoundsCobalt Compounds ; Nickel Compounds ; Edta ; Hydrates ; Magnetic Properties ; One−Dimensional Systems ; Ultralow Temperature ; Antiferromagnetism ; Magnetic Moments ; Exchange Interactions ; Ising Model ; Anisotropy ; Specific HeatMagnetic MomentsAntiferromagnetism:FÍSICA [UNESCO]AntiferromagnetismHydratesAnisotropyBimetallic stripAbsolute zeroSpin-½Condensed matter physicsMagnetic momentSpinsChemistryUNESCO::FÍSICAOne−Dimensional SystemsUltralow TemperatureSpecific HeatIsing ModelAnisotropyCondensed Matter::Strongly Correlated ElectronsIsing modelCobalt Compounds
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The ferrimagnetic compounds CoM[M’(EDTA)]2⋅4H2O(M,M’=Co,Ni): Magnetic characterization of CoCo[Ni(EDTA)2]⋅4H2O

1990

Under the terms of the Creative Commons Attribution (CC BY) license to their work.

Magnetic PropertiesExchange InteractionsEdtaNickel CompoundsGeneral Physics and AstronomyBimetalsFerrimagnetic MaterialsCondensed Matter::Materials ScienceNuclear magnetic resonance:FÍSICA [UNESCO]FerrimagnetismNickel compoundsCocoHydratesSpin (physics)Bimetallic stripChemistryUNESCO::FÍSICABimetals ; Magnetic Properties ; Exchange Interactions ; Cobalt Compounds ; Nickel Compounds ; Ferrimagnetic Materials ; Ising Model ; Edta ; HydratesCharacterization (materials science)CrystallographyIsing ModelOctahedronCondensed Matter::Strongly Correlated ElectronsIsing modelCobalt CompoundsJournal of Applied Physics
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Magnetic exchange interactions in the heteropoly complexes [M4(H2O)2(PW9O34)2]10− [M=Co(II) and Cu(II)]

1990

The magnetic properties of the heteropolyanions [M4(H2O)2(PW9O34)2]10− [M=Co(II) and Cu(II)] down to 4 K are reported. Their individual heteropoly molecules contain a rhomblike arrangement formed by four coplanar MO6 octahedra sharing edges. The magnetic properties support an intramolecular ferromagnetic exchange in the Co(II) tetramer, and antiferromagnetic exchange in the Cu(II) tetramer. These behaviors are discussed assuming anisotropic exchange in the Co(II) compound, and Heisenberg exchange in the Cu(II) compound. Carlos.Gomez@uv.es

Magnetic PropertiesExchange InteractionsGeneral Physics and AstronomyCopper ComplexesAntiferromagnetismTetramerVery Low TemperatureAntiferromagnetismMoleculeAnisotropy:FÍSICA::Química física [UNESCO]Cobalt Complexes ; Copper Complexes ; Heteropolyanions ; Magnetic Properties ; Exchange Interactions ; Ferromagnetism ; Antiferromagnetism ; Anisotropy ; Heisenberg Model ; Ultralow Temperature ; Very Low TemperatureCondensed matter physicsChemistryHeisenberg modelUltralow TemperatureUNESCO::FÍSICA::Química físicaCrystallographyOctahedronFerromagnetismIntramolecular forceFerromagnetismHeisenberg ModelAnisotropyCobalt ComplexesHeteropolyanions
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NEW SELF-ASSEMBLING POLYASPARTYLHYDRAZIDE COPOLYMER MICELLES FOR ANTICANCER DRUG DELIVERY.

2010

A new amphiphilic copolymer have been synthesized starting from the hydrosoluble polyaspartylhydrazide (PAHy) polymer, by grafting both hydrophilic PEG(2000) chains and hydrophobic palmitic acid (C(16)) moieties on polymer backbone, and the structure of obtained PAHy-PEG(2000)-C(16) copolymer have been characterized by 2D (1)H/(13)C NMR experiments. PAHy-PEG(2000)-C(16) copolymer showed the ability of self-assembling in aqueous media giving a core-shell structure and resulted potentially useful for encapsulating and dissolving hydrophobic drug. The formation of micellar core-shell structure has been investigated by 2D (1)H NMR NOESY experiments. The presence of cross-peaks for protons of C(…

Magnetic Resonance SpectroscopyLightCell SurvivalPolymersChemistry PharmaceuticalDrug CompoundingPalmitic AcidPharmaceutical ScienceAntineoplastic AgentsBreast NeoplasmsDRUG DELIVERY SELF ASSEMBLING POLYASPARTYLHYDRAZIDE MICELLES.MicelleFluorescencePolyethylene GlycolsDynamic light scatteringMicroscopy Electron TransmissionCell Line TumorAmphiphilePolymer chemistryCopolymerOrganic chemistryHumansNanotechnologyScattering RadiationTechnology PharmaceuticalSolubilityParticle SizeMicellesDrug CarriersDose-Response Relationship DrugChemistrytechnology industry and agricultureNuclear magnetic resonance spectroscopyHydrophobeTamoxifenSettore CHIM/09 - Farmaceutico Tecnologico ApplicativoFemaleDrug carrierPeptidesHydrophobic and Hydrophilic Interactions
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Water dynamics and its role in structural hysteresis of dissolved organic matter

2016

Knowledge of structural dynamics of dissolved organic matter (DOM) is of paramount importance for understanding DOM stability and role in the fate of solubilized organic and inorganic compounds (e.g., nutrients and pollutants), either in soils or aquatic systems. In this study, fast field cycling (FFC) (1)H NMR relaxometry was applied to elucidate structural dynamics of terrestrial DOM, represented by two structurally contrasting DOM models such as Suwanee River (SRFA) and Pahokee peat (PPFA) fulvic acids purchased by the International Humic Substance Society. Measurement of NMR relaxation rate of water protons in heating-cooling cycles revealed structural hysteresis in both fulvic acids. I…

Magnetic Resonance SpectroscopyrelaxometrySettore AGR/13 - Chimica Agraria010501 environmental sciences01 natural scienceshumic substanceSoilRiversDissolved organic carbonEnvironmental ChemistryReactivity (chemistry)Benzopyrans0105 earth and related environmental sciencesChemistryHydrogen bondwater histeresiChemical polarityTemperatureSoil chemistryWaterHydrogen Bonding04 agricultural and veterinary sciencesGeneral ChemistryNuclear magnetic resonance spectroscopyEnvironmental chemistrySoil water040103 agronomy & agricultureProton NMR0401 agriculture forestry and fisheriesHydrophobic and Hydrophilic Interactions
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