Search results for "Divalent"

showing 10 items of 102 documents

Interaction of Heparins and Dextran Sulfates with a Mesoscopic Protein Nanopore

2009

A mechanism of how polyanions influence the channel formed by Staphylococcus aureus alpha-hemolysin is described. We demonstrate that the probability of several types of polyanions to block the ion channel depends on the presence of divalent cations and the polyanion molecular weight and concentration. For heparins, a 10-fold increase in molecular weight decreases the half-maximal inhibitory concentration, IC(50), nearly 10(4)-fold. Dextran sulfates were less effective at blocking the channel. The polyanions are significantly more effective at reducing the conductance when added to the trans side of this channel. Lastly, the effectiveness of heparins on the channel conductance correlated wi…

Models MolecularStereochemistryBacterial ToxinsLipid BilayersMolecular ConformationBiophysicsmacromolecular substancesDivalentIonchemistry.chemical_compoundHemolysin ProteinsCysteineChannels and TransportersLipid bilayerIon channelchemistry.chemical_classificationMesoscopic physicsHeparinCell MembraneElectric Conductivitytechnology industry and agricultureConductanceDextransNanostructuresNanoporeDextranchemistryLiposomesMutationBiophysicsPorosityProtein BindingBiophysical Journal
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Chelate Cooperativity and Spacer Length Effects on the Assembly Thermodynamics and Kinetics of Divalent Pseudorotaxanes

2011

Homo- and heterodivalent crown-ammonium pseudorotaxanes with different spacers connecting the two axle ammonium binding sites have been synthesized and characterized by NMR spectroscopy and ESI mass spectrometry. The homodivalent pseudorotaxanes are investigated with respect to the thermodynamics of divalent binding and to chelate cooperativity. The shortest spacer exhibits a chelate cooperativity much stronger than that of the longer spacers. On the basis of crystal structure, this can be explained by a noninnocent spacer, which contributes to the binding strength in addition to the two binding sites. Already very subtle changes in the spacer length, i.e., the introduction of an additional…

Models Molecularchemistry.chemical_classificationSpectrometry Mass Electrospray IonizationMagnetic Resonance SpectroscopyRotaxanesCooperative bindingThermodynamicsCooperativityGeneral ChemistryCrystal structureNuclear magnetic resonance spectroscopyBiochemistryCatalysisDivalentQuaternary Ammonium CompoundsKineticschemistry.chemical_compoundColloid and Surface ChemistrychemistryIntramolecular forceEffective molarityThermodynamicsMethyleneta116Chelating AgentsJournal of the American Chemical Society
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Copper Uptake Induces Self-Assembly of 18.5 kDa Myelin Basic Protein (MBP)

2010

Myelin basic protein (MBP) is predominantly found in the membranes of the myelin sheath of the central nervous system and is involved in important protein-protein and protein-lipid interactions in vivo and in vitro. Furthermore, divalent transition metal ions, especially Zn(2+) and Cu(2+), seem to directly affect the MBP-mediated formation and stabilization of the myelin sheath of the central nervous system. MBP belongs to the realm of intrinsically disordered proteins, and only fragmentary information is available regarding its partial structure(s) or supramolecular arrangements. Here, using standard continuous wave and modern pulse electron paramagnetic resonance methods, as well as dynam…

Models Molecularinorganic chemicalsLightBiophysicsSupramolecular chemistryIn Vitro TechniquesIntrinsically disordered proteinsBiophysical PhenomenaDivalentlaw.inventionlawAnimalsScattering RadiationMoleculeParticle SizeElectron paramagnetic resonanceIon transporterchemistry.chemical_classificationIon TransportbiologyProteinElectron Spin Resonance SpectroscopyMyelin Basic ProteinMyelin basic proteinSolutionsZincMembranechemistryBiochemistrybiology.proteinBiophysicsCattleProtein MultimerizationCopperBiophysical Journal
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A Na+-coupled C4-dicarboxylate transporter (Asuc_0304) and aerobic growth of Actinobacillus succinogenes on C4-dicarboxylates

2014

Actinobacillus succinogenes, which is known to produce large amounts of succinate during fermentation of hexoses, was able to grow on C4-dicarboxylates such as fumarate under aerobic and anaerobic conditions. Anaerobic growth on fumarate was stimulated by glycerol and the major product was succinate, indicating the involvement of fumarate respiration similar to succinate production from glucose. The aerobic growth on C4-dicarboxylates and the transport proteins involved were studied. Fumarate was oxidized to acetate. The genome of A. succinogenes encodes six proteins with similarity to secondary C4-dicarboxylate transporters, including transporters of the Dcu (C4-dicarboxylate uptake), Dcu…

Molecular Sequence Datamedicine.disease_causeModels BiologicalMicrobiologyDivalentBacterial ProteinsFumaratesmedicineDicarboxylic AcidsAmino Acid SequenceAnaerobiosisCarbon RadioisotopesEscherichia coliPhylogenyDicarboxylic Acid Transporterschemistry.chemical_classificationbiologySodiumBiological TransportSuccinatesActinobacillusGene Expression Regulation BacterialFumarate reductasebiology.organism_classificationAerobiosisTransport proteinActinobacillus succinogenesGlucoseBiochemistrychemistrySymporterFermentationCotransporterSequence AlignmentMicrobiology
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The stability and functional properties of proteoliposomes mixed with dextran derivatives bearing hydrophobic anchor groups

1992

Liposomes composed of Escherichia coli phospholipid were coated with polysaccharides bearing hydrophobic palmitoyl anchors. The effect on the stability of liposomes without or with integral membrane proteins was investigated. A high concentration of hydrophobized dextrans protected the liposomes against detergent degradation, decreased the fluidity of the membranes, prevented fusion of the liposomes and enhanced their stability. Proteoliposomes containing beef heart cytochrome-c oxidase and the lactose transport carrier of E. coli were similarly affected by coating with the dextrans. Under these conditions both membrane proteins were still active. Long-term stability of the coated liposomes…

PROTEINMembrane FusionBiochemistryMembrane Potentialschemistry.chemical_compoundFUSIONINTEGRAL MEMBRANE PROTEINBINDINGIntegral membrane proteinLiposomeSymportersEscherichia coli ProteinsVesiclePROTEOLIPOSOMEDextransDEXTRAN DERIVATIVEBIOLOGICAL-MEMBRANESFluoresceinsMembraneCarbohydrate SequenceESCHERICHIA-COLIMonosaccharide Transport ProteinsCations DivalentMembrane FluidityProteolipidsMolecular Sequence DataBiophysicsPhospholipidFluorescence PolarizationLactose transportOXIDASECYTOCHROME-CVESICLESElectron Transport Complex IVHYDROPHOBIC ANCHOR GROUPEscherichia coliAnimalsKINETICSChromatographyMyocardiumMembrane ProteinsMembrane Transport ProteinsBiological membraneCell BiologyPROTON-MOTIVE FORCEMembrane proteinchemistryLiposomesCalciumCattleBiochimica et Biophysica Acta (BBA) - Biomembranes
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Divalent metal ion buffers with low pH-sensitivity

1973

Es werden Puffersysteme fur divalente Metallionen beschrieben, die im Bereich von etwa pH 6–10 gegenuber den herkommlichen Metallpuffern eine bemerkenswert niedrige pH-Abhangigkeit der Metallionenkonzentration und der Pufferkapazitat zeigen. Die Puffersysteme bestehen aus einem starken Komplexbildner (vorzugsweise einer Polyaminocarbonsaure) und zwei verschiedenen, divalenten Metallionen, die bezuglich der Bindung durch den Komplexbildner in Konkurrenz stehen. Dasjenige Metallion, dessen Konzentration gepuffert werden soll, wird als Primarion bezeichnet. Das zweite Ion, das Sekundarion genannt wird, soll vom Komplexbildner mindestens um den Faktor 10–100 schwacher gebunden werden. Die Gesam…

PharmacologyCellular and Molecular NeuroscienceChemistryDivalent metal ionsMolecular MedicineCell BiologyMolecular BiologyNuclear chemistryExperientia
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The molecular heterogeneity of hemocyanin: Structural and functional properties of the 4×6-meric protein of Upogebia pusilla (Crustacea)

2006

The structural properties of the hemocyanin isolated from the Mediterranean mud shrimp, Upogebia pusilla (Decapoda: Thalassinidea), were investigated. Our intent was to make use of the U. pusilla case to perform a structural comparison between crustacean and chelicerate 4×6-meric hemocyanins. The thalassinidean hemocyanin appears similar in size but different in structural organization compared to the chelicerate 4×6-mer. Ultracentrifuge analyses on the purified protein revealed a sedimentation coefficient of 39S, typical of 4×6 hemocyanins. Electron micrographs are in agreement with a model in which four 2×6-meric building blocks are arranged in a tetrahedron-like quaternary structure and …

Protein Conformation030310 physiologymedicine.medical_treatmentAllosteric regulationHemocyaninDivalent03 medical and health sciencesOxygen bindingDecapodaCatalytic propertiesGeneticsmedicineQuaternary structureAnimals030304 developmental biologychemistry.chemical_classification0303 health sciencesbiologyDecapodaHemocyaninGeneral Medicinebiology.organism_classificationHemocyanin; Quaternary structure; Dissociation; Oxygen binding; Catalytic propertiesMolecular WeightOxygenSedimentation coefficientMicroscopy ElectronchemistryBiochemistryHemocyaninsChromatography GelProtein quaternary structureUltracentrifugeDissociationOxygen bindingProtein BindingGene
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Thermal aggregation of beta-lactoglobulin in presence of metal ions.

2007

In this work, we report a study of the effects of zinc and copper ions on the heat-induced aggregation of beta-lactoglobulin (BLG). Kinetics investigations on aggregates growth by light scattering measurements and on secondary structure changes by FTIR absorption measurements show the different role played by the two metals during the whole process. In particular, the presence of zinc in solution promotes the formation of aggregates of BLG at a lower temperature than copper. Then, at fixed temperature, formation of a large amount of aggregates, of large dimension, is observed for Zn-BLG in shorter time; on the contrary, the presence of copper in solution does not affect the aggregation proc…

Protein DenaturationHot TemperatureCations DivalentMetal ions in aqueous solutionKineticsInorganic chemistryBiophysicsBeta-lactoglobulinchemistry.chemical_elementZincLactoglobulinsProtein aggregationBiochemistryProtein Structure SecondaryDivalentSpectroscopy Fourier Transform InfraredAnimalsMetal ionProtein secondary structurechemistry.chemical_classificationOrganic ChemistryLight scatteringCopperSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)FTIR spectroscopyKineticsZincchemistryChemical engineeringCattleAbsorption (chemistry)Protein aggregationCopperBiophysical chemistry
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Interference by toxic metal ions with zinc-dependent proteins involved in maintaining genomic stability.

2002

Metal ions are essential components of biological systems; nevertheless, even essential elements may have toxic or carcinogenic properties. Thus, besides As(III) and Cd(II), also Ni(II) and Co(II) have been shown previously to disturb different types of DNA repair systems at low, non-cytotoxic concentrations. Since some metals exert high affinities for SH groups, we investigated whether zinc finger structures in DNA-binding motifs of DNA repair proteins are potential targets for toxic metal ions. The bacterial formamidopyrimidine-DNA glycosylase (Fpg protein) involved in base excision repair was inhibited by Cd(II), Cu(II) and Hg(II) with increasing efficiencies, whereas Co(II), As(III), Pb…

Protein FoldingDNA RepairDNA repairCations DivalentPoly ADP ribose polymeraseToxicologymedicine.disease_causechemistry.chemical_compoundMetals HeavymedicineMetallothioneinHumansN-Glycosyl HydrolasesChemistryRNA-Binding ProteinsZinc FingersGeneral MedicineBase excision repairXeroderma Pigmentosum Group A ProteinDNA-Binding ProteinsZincBiochemistryDNA glycosylaseZinc toxicityDNAFood ScienceNucleotide excision repairFood and chemical toxicology : an international journal published for the British Industrial Biological Research Association
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New sulfonamide complexes with essential metal ions [Cu (II), Co (II), Ni (II) and Zn (II)]. Effect of the geometry and the metal ion on DNA binding …

2019

Abstract Mixed divalent Cu, Co, Ni and Zn complexes containing the new sulfonamide ligand N–(2–(pyridin–2–yl)ethyl)quinoline–8–sulfonamide (HQSEP) were prepared and characterized by physico-chemical techniques. The tetracoordinate [Cu(QSEP)X] [X = Br (1), Cl (2)] compounds present a seesaw geometry (τ4 = 0.56 (1) and 0.50 (2)). The Cu(II) in the [Cu(QSEP)(NO3)(MeOH)] (3) complex is five coordinate with a slightly distorted SP geometry (τ = 0.11). The [M(QSEP)(benz)] [M = Cu(II) (4), Ni(II) (5), Co(II) (6) and Zn(II) (7); benz = benzoate] compounds are configurationally isotypic. The coordination geometries of the M(II) ions can be best described as distorted SP (τ = 0.29, 0.15, 0.34 and 0.1…

Reaction mechanismMetal ions in aqueous solutionGeometry010402 general chemistry01 natural sciencesBiochemistryDivalentInorganic ChemistryMetalBovine serum albuminDNA Cleavagechemistry.chemical_classificationSulfonamidesDeoxyribonucleasesTetracoordinatebiology010405 organic chemistryChemistryLigandSerum Albumin BovineDNA0104 chemical sciencesSulfonamideMetalsvisual_artvisual_art.visual_art_mediumbiology.proteinJournal of inorganic biochemistry
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