Search results for "Solutions"

showing 10 items of 757 documents

Redox-responsive organometallic foldamers from ferrocene amino acid: Solid-phase synthesis, secondary structure and mixed-valence properties

2011

Oligoferrocenes Fmoc-Fca(n)-OMe (n=3-5) are assembled in a stepwise precise manner from Fmoc-protected ferrocene amino acid Fmoc-Fca-OH (H-Fca-OH = 1-amino-1'-ferrocene carboxylic acid; Fmoc = 9-fluorenylmethyloxycarbonyl) via amide bonds on solid supports by sequential Fmoc deprotection, acid activation and coupling steps. The resulting well-defined oligomers form ordered zigzag structures in THF solution with characteristic hydrogen bonding patterns. Electrochemical experiments reveal sequential oxidations of the individual ferrocene units in these peptides giving mixed-valent cations. Optical intervalence electron transfer is detected by intervalence transitions in the near-IR.

Models MolecularMetallocenesStereochemistryCarboxylic acidProtein Structure SecondaryInorganic Chemistrychemistry.chemical_compoundElectron transferSolid-phase synthesisPolymer chemistryOrganometallic CompoundsFerrous CompoundsAmino AcidsProtein secondary structurechemistry.chemical_classificationFluorenesValence (chemistry)Hydrogen bondSpectrum AnalysisDipeptidesAmino acidSolutionschemistryFerrocenePeptidomimeticsOxidation-ReductionDalton Transactions
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Synthesis and Self-Organization of Zinc β-(Dialkoxyphosphoryl)porphyrins in the Solid State and in Solution

2012

The first synthesis and self-organization of zinc β-phosphorylporphyrins in the solid state and in solution are reported. β-Dialkoxyphosphoryl-5,10,15,20-tetraphenylporphyrins and their Zn(II) complexes have been synthesized in good yields by using Pd- and Cu-mediated carbon-phosphorous bond-forming reactions. The Cu-mediated reaction allowed to prepare the mono-β-(dialkoxyphosphoryl)porphyrins 1 Zn-3 Zn starting from the β-bromo-substituted zinc porphyrinate ZnTPPBr (TPP = tetraphenylporphyrin) and dialkyl phosphites HP(O)(OR)(2) (R = Et, iPr, nBu). The derivatives 1 Zn-3 Zn were obtained in good yields by using one to three equivalents of CuI. When the reaction was carried out in the pres…

Models MolecularMetalloporphyrinschemistry.chemical_elementZincCrystallography X-Ray010402 general chemistryPhotochemistry01 natural sciencesCatalysisCatalysischemistry.chemical_compoundPolymer chemistryTetraphenylporphyrin[CHIM]Chemical SciencesComputingMilieux_MISCELLANEOUSMolecular Structure010405 organic chemistryOrganic ChemistryGeneral ChemistryNuclear magnetic resonance spectroscopyToluene0104 chemical sciencesSolutionsZincchemistryYield (chemistry)MethanolPalladiumChemistry - A European Journal
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Structural characterization of the Borrelia burgdorferi outer surface protein BBA73 implicates dimerization as a functional mechanism.

2013

Borrelia burgdorferi, which is the causative agent of Lyme disease, is transmitted from infected Ixodes ticks to a mammalian host following a tick bite. Upon changing the host organism from an Ixodes tick to a warm-blooded mammal, the spirochete must adapt to very different conditions, which is achieved by altering the expression of several genes in response to a changing environment. Recently, considerable attention has been devoted to several outer surface proteins, including BBA73, that undergo dramatic upregulation during the transmission of B. burgdorferi from infected Ixodes ticks to mammals and that are thought to be important for the establishment and maintenance of the infection. T…

Models MolecularMolecular Sequence DataStatic ElectricityBiophysicsCrystallography X-RayBiochemistryProtein Structure SecondaryMicrobiologyProtein structureAnimalsAmino Acid SequenceBorrelia burgdorferiCloning MolecularProtein Structure QuaternaryMolecular BiologyPeptide sequenceLyme DiseaseBinding SitesbiologyIxodesSequence Homology Amino AcidCell BiologyProtein superfamilyLigand (biochemistry)biology.organism_classificationSolutionsMembrane proteinBorrelia burgdorferiLyme disease microbiologyIxodesProtein MultimerizationBacterial Outer Membrane ProteinsBiochemical and biophysical research communications
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An efficient dissipative particle dynamics-based algorithm for simulating electrolyte solutions

2015

We propose an efficient simulation algorithm based on the dissipative particle dynamics (DPD) method for studying electrohydrodynamic phenomena in electrolyte fluids. The fluid flow is mimicked with DPD particles while the evolution of the concentration of the ionic species is described using Brownian pseudo particles. The method is designed especially for systems with high salt concentrations, as explicit treatment of the salt ions becomes computationally expensive. For illustration, we apply the method to electro-osmotic flow over patterned, superhydrophobic surfaces. The results are in good agreement with recent theoretical predictions.

Models MolecularOsmosisMaterials scienceSurface PropertiesGeneral Physics and AstronomyIonic bondingFOS: Physical sciencesElectrolyteCondensed Matter - Soft Condensed MatterIonPhysics::Fluid DynamicsElectrolytesFluid dynamicsPhysical and Theoretical ChemistryBrownian motionDissipative particle dynamicsFluid Dynamics (physics.flu-dyn)MechanicsPhysics - Fluid DynamicsComputational Physics (physics.comp-ph)SolutionsCondensed Matter::Soft Condensed MatterFlow (mathematics)HydrodynamicsSoft Condensed Matter (cond-mat.soft)SaltsElectrohydrodynamicsPhysics - Computational PhysicsHydrophobic and Hydrophilic InteractionsAlgorithms
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Detecting ni(ii) in aqueous solution by 3-(2-pyridyl)-[1,2,3]triazolo[1,5-a]pyridine and dimethyl-beta-cyclodextrin

2013

Abstract A new supramolecular sensitizer for nickel(II) ion in aqueous solution based on a pyridyltriazolopyridine-cyclodextrin inclusion complex is proposed. The inclusion complexation behavior, characterization and binding ability of pyridyltriazolopyridine (PTP) with dimethyl-β-cyclodextrin (DMβCD) has been investigated both in solution and solid state by means of absorption, fluorescence, 1H NMR, DSC, and molecular modeling methods. The stoichiometry of the inclusion complex is 1:1, and the thermodynamic studies indicate that the inclusion of PTP is mainly an entropic driven process. The 2D NMR studies revealed that the pyridyl-triazolopyridine is included by both sides of cyclodextrin …

Models MolecularPolymers and PlasticsPyridinesSupramolecular chemistryAnalytical chemistryMolecular ConformationDivalentchemistry.chemical_compoundNickelPyridineMaterials Chemistrychemistry.chemical_classificationAqueous solutionCyclodextrinChemistryOrganic Chemistrybeta-CyclodextrinsWaterTriazolesSolutionsProton NMRPhysical chemistrySelectivityTwo-dimensional nuclear magnetic resonance spectroscopyWater Pollutants ChemicalEnvironmental Monitoring
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Identifying three-way DNA junction-specific small-molecules

2012

Three-way junction DNA (TWJ-DNA, also known as 3WJ-DNA) is an alternative secondary DNA structure comprised of three duplex-DNAs that converge towards a single point, termed the branch point. This point is characterized by unique geometrical properties that make its specific targeting by synthetic small-molecules possible. Such a targeting has already been demonstrated in the solid state but not thoroughly biophysically investigated in solution. Herein, a set of simple biophysical assays has been developed to identify TWJ-specific small-molecule ligands; these assays, inspired by the considerable body of work that has been reported to characterize the interactions between small-molecules an…

Models MolecularPorphyrinsSolid-stateNanotechnologyComputational biology010402 general chemistryLigands01 natural sciencesBiochemistrySmall Molecule Libraries03 medical and health scienceschemistry.chemical_compoundPiperidinesFluorescence Resonance Energy TransferTransition TemperatureComputingMilieux_MISCELLANEOUS030304 developmental biology0303 health sciencesAza CompoundsSpectrum AnalysisGeneral MedicineDNASmall moleculePorphyrin0104 chemical sciencesG-QuadruplexesSolutions[SDV.BBM.BP]Life Sciences [q-bio]/Biochemistry Molecular Biology/BiophysicsKineticschemistryMetalsThree wayQuinolinesThermodynamicsSingle pointDNA
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Self-assembling of poly(aspartic acid) with bovine serum albumin in aqueous solutions

2016

Abstract Macromolecular co-assemblies built up in aqueous solutions, by using a linear polypeptide, poly(aspartic acid) (PAS), and a globular protein, bovine serum albumin (BSA), have been studied. The main interest was to identify the optimum conditions for an interpenetrated complex formation in order to design materials suitable for biomedical applications, such as drug delivery systems. BSA surface possesses several amino- and carboxylic groups available for covalent modification, and/or bioactive substances attachment. In the present study, mixtures between PAS and BSA were investigated at 37 °C in dilute aqueous solution by viscometry, dynamic light scattering and zeta potential deter…

Models MolecularProtein ConformationGlobular protein02 engineering and technology010402 general chemistry01 natural sciencesBiochemistryDynamic light scatteringStructural BiologyAspartic acidZeta potentialAnimalsBovine serum albuminMolecular Biologychemistry.chemical_classificationAqueous solutionChromatographybiologyChemistryWaterSerum Albumin BovineGeneral MedicineHydrogen-Ion Concentration021001 nanoscience & nanotechnology0104 chemical sciencesSolutionsDrug deliverybiology.proteinCattlePeptides0210 nano-technologyProtein BindingNuclear chemistryMacromoleculeInternational Journal of Biological Macromolecules
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Cytochrome c in a Dry Trehalose Matrix: Structural and Dynamical Effects Probed by X-Ray Absorption Spectroscopy

2007

AbstractWe report on the structure and dynamics of the Fe ligand cluster of reduced horse heart cytochrome c in solution, in a dried polyvinyl alcohol (PVA) film, and in two trehalose matrices characterized by different contents of residual water. The effect of the solvent/matrix environment was studied at room temperature using Fe K-edge x-ray absorption fine structure (XAFS) spectroscopy. XAFS data were analyzed by combining ab initio simulations and multi-parameter fitting in an attempt to disentangle structural from disorder parameters. Essentially the same structural and disorder parameters account adequately for the XAFS spectra measured in solution, both in the absence and in the pre…

Models MolecularProtein ConformationIronAb initioBiophysicsHemechemistry.chemical_compoundProtein structureImidazoleAnimalsHistidineHorsesSpectroscopyX-ray absorption spectroscopyMyocardiumSpectrum AnalysisX-RaysProteinsCytochromes cTrehaloseTrehaloseX-ray absorption fine structureSolutionsCrystallographychemistryPolyvinyl AlcoholAbsorption (chemistry)Biophysical Journal
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QM/MM calculations of kinetic isotope effects in the chorismate mutase active site.

2003

Kinetic isotope effects have been computed for the Claisen rearrangement of chorismate to prephenate in aqueous solution and in the active site of chorismate mutase from B. subtilus. These included primary 13C and 18O and secondary 3H effects for substitutions at the bond-making and bond-breaking positions. The initial structures of the putative stationary points on the potential energy surface, required for the calculations of isotope effects using the CAMVIB/CAMISO programs, have been selected from hybrid QM/MM molecular dynamical simulations using the DYNAMO program. Refinement of the reactant complex and transition-state structures has been carried out by means of AM1/CHARMM24/TIP3P cal…

Models MolecularProtein ConformationKinetic schemeBiochemistryCatalysisQM/MMIsotopesComputational chemistryKinetic isotope effectComputer SimulationPhysical and Theoretical ChemistryAqueous solutionBinding SitesbiologyChemistryOrganic ChemistryActive siteClaisen rearrangementSolutionsKineticsPotential energy surfacebiology.proteinChorismate mutaseQuantum TheoryThermodynamicsGasesSoftwareBacillus subtilisChorismate MutaseOrganicbiomolecular chemistry
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NMR Solution Structure of the Non-RGD Disintegrin Obtustatin

2003

The solution structure of obtustatin, a novel non-RGD disintegrin of 41 residues isolated from Vipera lebetina obtusa venom, and a potent and selective inhibitor of the adhesion of integrin alpha(1)beta(1) to collagen IV, has been determined by two-dimensional nuclear magnetic resonance. Almost the whole set of chemical shifts for 1H, 13C and 15N were assigned at natural abundance from 2D homonuclear and heteronuclear 500 MHz, 600 MHz and 800 MHz spectra at pH 3.0 recorded at 298 K and 303 K. Final structural constraints consisted of 302 non-redundant NOE (95 long-range, 60 medium, 91 sequential and 56 intra-residue), four disulfide bond distances, five chi1 dihedral angles and four hydroge…

Models MolecularProtein ConformationStereochemistryDisintegrinsMolecular Sequence DataStatic ElectricityViper VenomsDihedral angleCrystallography X-RayStructural BiologyDisintegrinAnimalsAmino Acid SequenceNuclear Magnetic Resonance BiomolecularMolecular BiologyProtein secondary structureConformational isomerismRGD motifMolecular StructureSequence Homology Amino AcidbiologyHydrogen bondChemistryCircular DichroismChemical shiftHydrogen BondingHydrogen-Ion ConcentrationSolutionsKineticsHeteronuclear moleculebiology.proteinOligopeptidesJournal of Molecular Biology
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