Search results for "Ternary complex"

showing 10 items of 16 documents

Modulating the DNA cleavage ability of copper(II) Schiff bases through ternary complex formation

2018

Copper(II) complexes with the potentially tridentate Schiff bases N-[(3-ethoxy-2-hydroxyphenyl)methylidene]-N′-tosylbenzene-1,2-diamine (H2L1) and N-[(2-hydroxynaphthanyl)methylidene]-N′-tosylbenzene-1,2-diamine (H2L2) have been synthesized by electrochemical oxidation of the metal in an electrochemical cell containing a solution of the corresponding ligand in acetonitrile. Adducts of these compounds with 2,2′-bipyridine (2,2′-bpy), 4,4′-bipyridine (4,4′-bpy) or 1,10-phenanthroline (phen) were also obtained. The complexes have been characterized by microanalysis, mass spectrometry, EPR, IR and UV-Vis spectroscopies, as well as DFT calculations. The ligand H2L1 and the compounds [CuL1(H2O)]·…

010405 organic chemistrySupramolecular chemistrychemistry.chemical_elementNANOPARTÍCULASGeneral Chemistry010402 general chemistry01 natural sciencesCopperCatalysisSquare pyramidal molecular geometry0104 chemical scienceslaw.inventionAdductMetalCrystallographychemistry.chemical_compoundchemistrylawvisual_artMaterials Chemistryvisual_art.visual_art_mediumElectron paramagnetic resonanceAcetonitrileTernary complex
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Structural and mechanistic insights into the interaction of the circadian transcription factor BMAL1 with the KIX domain of the CREB-binding protein

2019

JBC papers in press xx, 16604-16619 (2019). doi:10.1074/jbc.RA119.009845

0301 basic medicineendocrine systemCircadian clockTranscription factor complex610BiochemistryProtein Structure SecondaryProtein–protein interaction03 medical and health sciencesTransactivationMiceProto-Oncogene Proteins c-mybProtein DomainsX-Ray DiffractionCircadian ClocksScattering Small AngleAnimalsddc:610Amino Acid SequenceCREB-binding proteinMolecular BiologyTernary complexTranscription factorBinding Sites030102 biochemistry & molecular biologybiologyChemistryARNTL Transcription FactorsCell BiologyHistone-Lysine N-MethyltransferaseSurface Plasmon ResonanceCREB-Binding ProteinRecombinant ProteinsCell biologyProtein Structure Tertiary030104 developmental biologyStructural biologyProtein Structure and Foldingbiology.proteinMutagenesis Site-DirectedMyeloid-Lymphoid Leukemia ProteinProtein Binding
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Can copper(II) mediate Hoogsteen base-pairing in a left-handed DNA duplex? A pulse EPR study

2010

Pulse EPR spectroscopy is sued to investigate possible structural features of the copper(II) ion coordinated to poly(dG-dC) poly(dG-dC) in a frozen aqueous solution, and the structural change of the polynucleotide induced by the presence of the metal ion. Two different copper species were identified and their geometry explained by a molecular model. According to this model, one species is exclusively coordinated to a single guanine with the N7 nitrogen atom forming a coordinative bond with the copper. In the other species, a guanine and a cytosine form a ternary complex together with the copper ion. A copper crosslink between the N7 of guanine and N3 of cytosine is proposed as the most prob…

10120 Department of ChemistryCircular dichroismGuanineStereochemistryHoogsteen base pairrame strutture del DNA basi nucleotidiche EPR a impulsi risonanza paramagneticachemistry.chemical_elementTriple-stranded DNA3107 Atomic and Molecular Physics and OpticsNucleobasechemistry.chemical_compoundPolydeoxyribonucleotidesDNA structures540 ChemistryDNA Z-FormPhysical and Theoretical ChemistryBase PairingTernary complexCircular Dichroismstructure elucidationElectron Spin Resonance Spectroscopypulse EPIR spectroscopynucleobasesCopperSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)Atomic and Molecular Physics and Opticschemistrycopper1606 Physical and Theoretical ChemistryCytosine
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Flow spectrophotometric determination of ammonium ion

1999

Abstract A flow procedure is proposed for the determination of ammonium ion. The sample in basic medium is forced through a solid-phase reactor containing immobilized AgCl on polymeric pearl beads. The released Ag + , complexed with the ammonia, gives a blue ternary complex with the aid of bromopyrogallol red and 1,10-phenanthroline which is spectrophotometrically monitored at 636 nm. The calibration graph is linear over the range 1–20 μg ml −1 ammonium ion, detection limit ( s / n  = 3)  0.35 μg ml −1 and relative standard deviation (slope) 1.9 % ( n  = 7). The sample throughput is 48 h −1 . The influence of foreign compounds is studied and the procedure is applied to ammonium ion determi…

Detection limitBromopyrogallol redChemistryCalibration curveAnalytical chemistryBiochemistryAnalytical ChemistryIonAmmoniachemistry.chemical_compoundSilver chlorideEnvironmental ChemistryAmmoniumTernary complexSpectroscopyNuclear chemistryAnalytica Chimica Acta
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Topologically Controlled Interpolyelectrolyte Complexes

2008

The complexation of a cylindrical polyelectrolyte−brush−surfactant complex (PMMPSS−C12) and an oppositely, highly charged cylindrical polyelectrolyte−brush (PMMPEI−PEO) in dimethylformamide (DMF) l...

Inorganic Chemistrychemistry.chemical_compoundPolymers and PlasticschemistryOrganic ChemistryPolymer chemistryMaterials ChemistryRadius of gyrationCopolymerDimethylformamideTernary complexPolyelectrolyteMacromolecules
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Molecular Motions within Self-Assembled Dimeric Capsules with Tetraethylammonium Cations as Guest

2001

Hydrogen-bonded, dimeric capsules of calix[4]arenes substituted at the wide rim by four urea functions show unprecedented dynamic features when a tetraethylammonium cation is included as a guest. The seam of hydrogen bonds C=O...(HN)2C=O in the equatorial region which holds the two calixarene counterparts together changes its directionality fast (at 25 degrees C), while the dimer itself is kinetically stable on the NMR time scale. An energy barrier of deltaG++ = 49.9 kJmol(-1) (Tc 276 K) was estimated for this reorientation from variable-temperature (VT) NMR measurements. Lowering the temperature to about -50 degrees C restricts also the rotation of the encapsulated tetraethylammonium catio…

Magnetic Resonance SpectroscopyTetraethylammoniumMacromolecular SubstancesHydrogen bondDimerOrganic ChemistryTetraethylammoniumHydrogen BondingGeneral ChemistryNuclear magnetic resonance spectroscopyInteraction energyCatalysischemistry.chemical_compoundCrystallographychemistryCalixareneProton NMRThermodynamicsCalixarenesDimerizationTernary complexChemistry - A European Journal
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Unraveling the Reaction Mechanism of Enzymatic C5-Cytosine Methylation of DNA. A Combined Molecular Dynamics and QM/MM Study of Wild Type and Gln119 …

2016

M.HhaI is a DNA methyltransferase from Haemophilus hemolyticus that catalyzes the transfer of a methyl group from S-adenosyl-l-methionine (SAM) to the C5 position of a cytosine. This enzyme is a paradigmatic model for C5 DNA methyltransferases due to its major homology to mammalian enzymes and to the availability of high-resolution structures of the DNA–enzyme complex. In spite of the number of experimental and theoretical analyses carried out for this system, many mechanistic details remain unraveled. We have used full atomistic classical molecular dynamics simulations to explore the protein–SAM–DNA ternary complex, where the target cytosine base is flipped out into the active site for bot…

MethyltransferaseStereochemistry010402 general chemistry01 natural sciencesMolecular mechanicsenzyme catalysisCatalysisQM/MMchemistry.chemical_compound0103 physical sciencesA-DNATernary complex010304 chemical physicsbiologyChemistryActive siteGeneral Chemistryfree energy profiles0104 chemical sciencesreaction mechanismsBiochemistrybiology.proteinQM/MM methodsstring methodDNA-methylationCytosineDNA
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A Quantum Mechanic/Molecular Mechanic Study of the Wild-Type and N155S Mutant HIV-1 Integrase Complexed with Diketo Acid

2008

Integrase (IN) is one of the three human immunodeficiency virus type 1 (HIV-1) enzymes essential for effective viral replication. Recently, mutation studies have been reported that have shown that a certain degree of viral resistance to diketo acids (DKAs) appears when some amino acid residues of the IN active site are mutated. Mutations represent a fascinating experimental challenge, and we invite theoretical simulations for the disclosure of still unexplored features of enzyme reactions. The aim of this work is to understand the molecular mechanisms of HIV-1 IN drug resistance, which will be useful for designing anti-HIV inhibitors with unique resistance profiles. In this study, we use mo…

Models MolecularProtein ConformationStereochemistryBiophysicsIntegrase inhibitorIntegrase InhibitorsHIV IntegraseBiophysical Theory and ModelingMechanicsMolecular mechanicsProtein structureComputer SimulationMagnesiumTernary complexBinding SitesbiologyChemistryAminobutyratesWild typeActive siteLigand (biochemistry)PhenylbutyratesIntegraseModels ChemicalMultiprotein ComplexesMutagenesis Site-Directedbiology.proteinQuantum TheoryProtein BindingBiophysical Journal
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The membrane distal half of gp130 is responsible for the formation of a ternary complex with IL-6 and the IL-6 receptor

1995

AbstractGp130 is the signal transducing subunit of the interleukin-6 receptor. Signaling is initiated by the complex formation of gp130 with IL-6 bound to the IL-6 receptor (IL-6R). We have subdivided the extracellular domain of gp130 in two parts and expressed the mutant proteins as soluble IgG fusion proteins in COS-7 cells. By studying the formation of the ternary complex we show that the membrane distal half of gp130 which contains a cytokine receptor domain is responsible for the interaction with the IL-6/IL-6R complex. Interestingly this is the same region which is believed to be involved in specific recognition of the related cytokines LIF, OM, and probably also of CNTF and IL-11.

Molecular Sequence DataBiophysicsBiologyBiochemistryCytokine receptor domainCell Linegp130Structure-function analysisAntigens CDStructural BiologyCytokine Receptor gp130GeneticsAnimals5-HT5A receptorReceptorMolecular BiologyTernary complexMembrane GlycoproteinsBase SequenceInterleukin-6digestive oral and skin physiologyHaplorhiniReceptors InterleukinCell BiologyGlycoprotein 130Receptors Interleukin-6Fusion proteinbiological factorsCell biologyOligodeoxyribonucleotidesInterleukin-6 receptorCancer researchSignal transductionCytokine receptorProtein BindingSignal TransductionFEBS Letters
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Dynamics and reactivity in Thermus aquaticus N6-adenine methyltransferase.

2014

M.TaqI is a DNA methyltransferase from Thermus aquaticus that catalyzes the transfer of a methyl group from S-adenosyl-l-methionine to the N6 position of an adenine, a process described only in prokaryotes. We have used full atomistic classical molecular dynamics simulations to explore the protein–SAM–DNA ternary complex where the target adenine is flipped out into the active site. Key protein–DNA interactions established by the target adenine in the active site are described in detail. The relaxed structure was used for a combined quantum mechanics/molecular mechanics exploration of the reaction mechanism using the string method. According to our free energy calculations the reaction takes…

Reaction mechanismSite-Specific DNA-Methyltransferase (Adenine-Specific)BioinformaticsStereochemistryProtein ConformationMolecular Dynamics SimulationBiochemistryCatalysisMolecular dynamicschemistry.chemical_compoundColloid and Surface ChemistryReaction rate constantAbstractingA-DNAThermusTernary complexThermus aquaticusbiologyActive siteGeneral ChemistryDNAbiology.organism_classificationchemistryFunctional groupsbiology.proteinAmino acidsNucleic Acid ConformationQuantum TheoryThermodynamicsMethyl groupJournal of the American Chemical Society
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