Search results for " Divalent"

showing 10 items of 33 documents

Geometric Isomerism in Pentacoordinate Cu2+ Complexes: Equilibrium, Kinetic, and Density Functional Theory Studies Reveal the Existence of Equilibriu…

2009

A ligand (L1) (bis(aminoethyl)[2-(4-quinolylmethyl)aminoethyl]amine) containing a 4-quinolylmethyl group attached to one of the terminal amino groups of tris(2-aminoethyl)amine (tren) has been prepared, and its protonation constants and stability constants for the formation of Cu(2+) complexes have been determined. Kinetic studies on the formation of Cu(2+) complexes in slightly acidic solutions and on the acid-promoted complex decomposition strongly suggest that the Cu(2+)-L1 complex exists in solution as a mixture of two species, one of them showing a trigonal bipyramidal (tbp) coordination environment with an absorption maximum at 890 nm in the electronic spectrum, and the other one bein…

Models MolecularMagnetic Resonance SpectroscopyCations DivalentMolecular ConformationProtonationLigandsInorganic ChemistryIsomerismComputational chemistryMoleculePhysical and Theoretical ChemistryMolecular StructureChemistryLigandHydrolysisNuclear magnetic resonance spectroscopyHydrogen-Ion ConcentrationSquare pyramidal molecular geometryKineticsTrigonal bipyramidal molecular geometryCrystallographySpectrophotometryDensity functional theoryProtonsAcidsCopperCis–trans isomerismInorganic Chemistry
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Atomic structure of the major capsid protein of rotavirus: implications for the architecture of the virion

2001

The structural protein VP6 of rotavirus, an important pathogen responsible for severe gastroenteritis in children, forms the middle layer in the triple-layered viral capsid. Here we present the crystal structure of VP6 determined to 2 A resolution and describe its interactions with other capsid proteins by fitting the atomic model into electron cryomicroscopic reconstructions of viral particles. VP6, which forms a tight trimer, has two distinct domains: a distal beta-barrel domain and a proximal alpha-helical domain, which interact with the outer and inner layer of the virion, respectively. The overall fold is similar to that of protein VP7 from bluetongue virus, with the subunits wrapping …

Models MolecularRotavirusCations DivalentViral proteinvirusesMolecular Sequence DataHemagglutinins ViralTrimerCrystal structureBiologyCrystallography X-Raymedicine.disease_causeProtein Structure SecondaryArticleGeneral Biochemistry Genetics and Molecular BiologyVirus03 medical and health sciencesCapsidRotavirusAtomic modelmedicineAnimalsAmino Acid SequenceAntigens ViralMolecular BiologyPeptide sequence030304 developmental biology0303 health sciencesSequence Homology Amino AcidGeneral Immunology and Microbiology030306 microbiologyViral Core ProteinsGeneral NeuroscienceVirionvirus diseasesMolecular biologyZincCapsidSolventsBiophysicsCapsid ProteinsCattleThe EMBO Journal
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Coordination of Cu2+ Ions to C2 Symmetric Pseudopeptides Derived from Valine

2010

The acid-base and coordination properties of a family of pseudopeptidic ligands with C(2) symmetry derived from valine (4a-e) have been studied using a variety of techniques as a model for metal coordination in peptides and proteins. The Cu(2+) cation has been selected for coordination studies, although, for comparison, some results for Zn(2+) are also presented. Good agreement has been obtained between the results obtained by potentiometric titrations, spectroscopic analysis, and mass spectrometry (ESI) studies. These results highlight the potential for the use of ESI MS for characterizing the nature of the complex species formed. Clearly, the Cu(2+) complexes are much more stable than the…

Models MolecularSpectrometry Mass Electrospray IonizationMagnetic Resonance SpectroscopyCations DivalentChemistryStereochemistryCu2 ionsValineCrystallography X-RayInorganic ChemistryMetalZincCrystallographyCoordination ComplexesValinevisual_artvisual_art.visual_art_mediumProtonsPhysical and Theoretical ChemistrySymmetry (geometry)CopperInorganic Chemistry
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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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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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Development of a biosensor for copper detection in aqueous solutions using an Anemonia sulcata recombinant GFP.

2014

Fluorescent proteins from marine organisms represent potential candidates for biosensor development. In this paper, we described the isolation of a native green fluorescent protein from Anemonia sulcata and the cloning and purification of its equivalent as a recombinant protein in Escherichia coli. Furthermore, the spectroscopic behaviours of the native and recombinant GFPs were investigated as a function of Cu2+, Cd2+, Pb 2+ and Ni2+ concentration. Our results suggest the high selectivity of both proteins at copper than the other metals and, for the recombinant protein, a great sensitivity at a very low concentration (0.1-1 μM). Moreover, starting from these data, using the combination of …

Recombinant proteinGreen Fluorescent Proteinschemistry.chemical_elementBioengineeringBiosensing Techniquesmedicine.disease_causeApplied Microbiology and BiotechnologyBiochemistrylaw.inventionGreen fluorescent proteinlawQuenchingmedicineEscherichia coliAnimalsGreen fluorescent proteinMolecular BiologyEscherichia coliQuenching (fluorescence)Aqueous solutionChromatographyChemistryDivalent metal ionCopper; Detector; Divalent metal ions; Green fluorescent protein; Quenching; Recombinant proteinDetectorGeneral MedicineFluorescenceCopperSea AnemonesRecombinant DNABiosensorCopperBiotechnologyApplied biochemistry and biotechnology
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Metal complexes of the carbonic anhydrase inhibitor methazolamide (Hmacm). Crystal structure of the Zn(macm)2 (NH3)2. Anticonvulsant properties of th…

1995

Complexes of Co(II), Cu(II), and Zn(II) with deprotonated methazolamide and ammonia are synthesized and characterized. The complex Zn(macm)2(NH3)2 crystallizes in the monoclinic C2/c space group with a = 13.468(1), b = 6.759(1), c = 23.014(2) A, beta = 90.27(1), and Z = 4. The structure was refined to R = 0.049 (Rw = 0.053). The Zn(II) ion is coordinated to two deprotonated sulfonamido nitrogen atoms of the macm- ligand and two nitrogen atoms of the ammonia ligands in a distorted tetrahedron. The Zn(macm)2(NH3)2 complex is shown to be a simple model for the methazolamide inhibition of CA. EHMO calculations applied to fractional coordinates of the Zn(macm)2(NH3)2 complex indicate that the at…

Spectrophotometry InfraredCations DivalentInorganic chemistryMethazolamidechemistry.chemical_elementCrystal structureZincCrystallography X-RayBiochemistryInorganic ChemistryMetalDeprotonationmedicineAnimalsMethazolamideHOMO/LUMOMolecular StructureChemistryLigandElectron Spin Resonance SpectroscopyCobaltZincCrystallographyvisual_artvisual_art.visual_art_mediumAnticonvulsantsCoppermedicine.drugMonoclinic crystal systemJournal of Inorganic Biochemistry
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The purification and properties of nucleoside phosphotransferase from mucosa of chicken intestine

1984

Abstract (1) Nucleoside phosphotransferase (nucleotide:3′-deoxynucleoside 5′-phosphotransferase, EC 2.7.1.77) has been purified from chicken intestine mucosa to apparent homogeneity. The enzyme is represented by a multisubunit protein at different degrees of association. It can dissociate into a compoenent with a marked fall in catalytic activity. (2) The associated forms are similar to the enzyme previously purified from chick embryo as regards: substrate specificity both with respect to nucleoside monophosphate donors and to deoxyribonucleoside acceptors; sigmoidicity in the rate curve with a variable phosphate donor; instability to heat, dilution and lowering of pH; the activating and pr…

StereochemistryCations DivalentProtein subunitBiophysicsBiologyBiochemistrychemistry.chemical_compoundStructural BiologySettore BIO/10 - BiochimicaNucleoside phosphotransferaseCentrifugation Density GradientAnimalsUreaNucleotideEnzyme kineticsIntestinal MucosaMolecular Biologychemistry.chemical_classificationNucleotidesPhosphotransferasesPhosphatenucleoside phosphotransferaseDeoxyuridineDeoxyribonucleosideMolecular WeightKineticsEnzymechemistryBiochemistryAlcoholsChromatography GelElectrophoresis Polyacrylamide GelChickens
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Supramolecular assemblies of phenyl-pyridyl-triazolopyridine and β-cyclodextrin as sensor of divalent cations in aqueous solution

2014

The chemosensor 3-phenyl-7-(pyrid-2-yl)-[1,2,3]triazolo[1,5-a]pyridine (PhPTP) used in combination with two different cyclodextrins, enable its solubilization and stabilization in aqueous solution. The behavior of the inclusion complex, and its binding ability in both cyclodextrins were investigated by means of absorption and fluorescence spectroscopy. The best results were obtained for PhPTP-DMβCD assembly, and its orientation in the DMβCD nano cavity was obtained by 2D-NMR. This inclusion geometry was confirmed by docking studies. The binary complex was proved as chemosensor upon the presence of different divalent cations in aqueous solutions. The PhPTP-DMβCD system, displays a high sensi…

chemistry.chemical_classificationAqueous solutionPolymers and PlasticsCyclodextrinCations DivalentPyridinesIronbeta-CyclodextrinsOrganic ChemistryInorganic chemistrySupramolecular chemistryWaterTriazolesFluorescenceFluorescenceFluorescence spectroscopyNanostructuresDivalentchemistry.chemical_compoundchemistryPyridinePolymer chemistryMaterials ChemistryTriazolopyridineCarbohydrate Polymers
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