Search results for "surface properties"

showing 10 items of 421 documents

Active surfaces engineered by immobilizing protein-polymer nanoreactors for selectively detecting sugar alcohols.

2016

We introduce active surfaces generated by immobilizing protein-polymer nanoreactors on a solid support for sensitive sugar alcohols detection. First, such selective nanoreactors were engineered in solution by simultaneous encapsulation of specific enzymes in copolymer polymersomes, and insertion of membrane proteins for selective conduct of sugar alcohols. Despite the artificial surroundings, and the thickness of the copolymer membrane, functionality of reconstituted Escherichia coli glycerol facilitator (GlpF) was preserved, and allowed selective diffusion of sugar alcohols to the inner cavity of the polymersome, where encapsulated ribitol dehydrogenase (RDH) enzymes served as biosensing e…

Models MolecularMaterials scienceMembrane permeabilityPolymersSurface PropertiesBiophysicsBioengineering02 engineering and technologyNanoreactorBiosensing Techniques010402 general chemistryRibitolAquaporins01 natural sciencesPermeabilityBiomaterialschemistry.chemical_compoundSugar AlcoholsEscherichia coliOrganic chemistrySugar alcoholRibitolchemistry.chemical_classificationEscherichia coli Proteins021001 nanoscience & nanotechnology0104 chemical sciencesNanostructuresMembraneImmobilized ProteinschemistryMechanics of MaterialsPolymersomeCeramics and Composites0210 nano-technologyBiosensorSugar Alcohol DehydrogenasesSugar Alcohol DehydrogenasesBiomaterials
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Silicic acid competes for dimethylarsinic acid (DMA) immobilization by the iron hydroxide plaque mineral goethite.

2015

Abstract A surface complexation modeling approach was used to extend the knowledge about processes that affect the availability of dimethylarsinic acid (DMA) in the soil rhizosphere in presence of a strong sorbent, e.g., Fe plaques on rice roots. Published spectroscopic and molecular modeling information suggest for the organoarsenical agent to form bidentate-binuclear inner-sphere surface complexes with Fe hydroxides similar to the inorganic As oxyanions. However, since also the ubiquitous silicic acid oxyanion form the same bidentate binuclear surface complexes, our hypothesis was that it may have an effect on the adsorption of DMA by Fe hydroxides in soil. Our experimental batch equilibr…

Models MolecularMineralsEnvironmental EngineeringGoethiteSorbentSurface PropertiesInorganic chemistrySilicic AcidOxyanionPollutionAcid dissociation constantchemistry.chemical_compoundAdsorptionchemistryvisual_artvisual_art.visual_art_mediumEnvironmental ChemistryHydroxideCacodylic AcidSilicic acidPoint of zero chargeAdsorptionWaste Management and DisposalIron CompoundsThe Science of the total environment
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Comparison of the decameric structure of peroxiredoxin-II by transmission electron microscopy and X-ray crystallography

2001

Abstract The decameric human erythrocyte protein torin is identical to the thiol-specific antioxidant protein-II (TSA-II), also termed peroxiredoxin-II (Prx-II). Single particle analysis from electron micrographs of Prx-II molecules homogeneously orientated across holes in the presence of a thin film of ammonium molybdate and trehalose has facilitated the production of a ≥20 A 3-D reconstruction by angular reconstitution that emphasises the D5 symmetry of the ring-like decamer. The X-ray structure for Prx-II was fitted into the transmission electron microscopic reconstruction by molecular replacement. The surface-rendered transmission electron microscopy (TEM) reconstruction correlates well…

Models MolecularMolybdenumErythrocytesSurface PropertiesCryo-electron microscopyChemistryResolution (electron density)BiophysicsTrehaloseSingle particle analysisPeroxiredoxinsCrystallography X-RayBiochemistryNegative stainMicroscopy ElectronCrystallographyPeroxidasesElectron tomographyStructural BiologyTransmission electron microscopyHumansEnergy filtered transmission electron microscopyOrthorhombic crystal systemMolecular BiologyBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
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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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Dynamics of surface of lipid membranes: theoretical considerations and the ESR experiment.

2016

The effect of the surface layer of model membranes on their physical properties was discussed in this paper. The research involved a physical ESR experiment with the use of spin probes and computer simulation based on the Monte Carlo technique. Liposomes formed during the process of sonication of lecithin were scanned in an ESR spectrometer. The membrane surface layer model, represented by the system of electric dipoles arranged in rectangular or hexagonal matrices, was studied. The final states of computer simulations were presented as textures. It was found that in the gel phase some ordered domain structures are formed, while in the liquid–crystal phase we got complex textures comprising…

Models MolecularPhase transition12-DipalmitoylphosphatidylcholineSurface PropertiesMonte Carlo methodBiophysicsAnalytical chemistryMolecular Conformation02 engineering and technologyPhase Transition03 medical and health sciencesSonication0302 clinical medicinePhase (matter)Lipid membraneSurface layerMembrane fluidityLipid bilayerMonte Carlo simulationChemistryCell MembraneElectron Spin Resonance SpectroscopyTemperatureGeneral MedicineHydrogen-Ion ConcentrationESR probe021001 nanoscience & nanotechnologyElectric dipole momentDipoleKineticsMembraneChemical physics030220 oncology & carcinogenesisLiposomesOriginal Article0210 nano-technologyMonte Carlo MethodEuropean biophysics journal : EBJ
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Ligand-Stabilized Au13Cux (x = 2, 4, 8) Bimetallic Nanoclusters: Ligand Engineering to Control the Exposure of Metal Sites

2013

Three novel bimetallic Au-Cu nanoclusters stabilized by a mixed layer of thiolate and phosphine ligands bearing pyridyl groups are synthesized and fully characterized by X-ray single crystal analysis and density functional theory computations. The three clusters have an icosahedral Au13 core face-capped by two, four, and eight Cu atoms, respectively. All face-capping Cu atoms in the clusters are triply coordinated by thiolate or pyridyl groups. The surface ligands control the exposure of Au sites in the clusters. In the case of the Au13Cu8 cluster, the presence of 12 2-pyridylthiolate ligands still leaves open space for catalysis. All the 3 clusters are 8-electron superatoms displaying opti…

Models MolecularPhosphinesPyridinesSurface PropertiesInorganic chemistryMetal NanoparticlesCrystal structureLigandsBiochemistryCatalysisNanoclusterschemistry.chemical_compoundColloid and Surface ChemistryCluster (physics)Sulfhydryl CompoundsBimetallic stripta214ta114LigandThermal decompositionGeneral ChemistryCrystallographychemistryQuantum TheoryDensity functional theoryGoldCopperPhosphineJournal of the American Chemical Society
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Origins of fluorescence in evolved bacteriophytochromes

2014

Use of fluorescent proteins to study in vivo processes in mammals requires near-infrared (NIR) biomarkers that exploit the ability of light in this range to penetrate tissue. Bacteriophytochromes (BphPs) are photoreceptors that couple absorbance of NIR light to photoisomerization, protein conformational changes, and signal transduction. BphPs have been engineered to form NIR fluorophores, including IFP1.4, Wi-Phy, and the iRFP series, initially by replacement of Asp-207 by His. This position was suggestive because its main chain carbonyl is within hydrogen-bonding distance to pyrrole ring nitrogens of the biliverdin chromophore, thus potentially functioning as a crucial transient proton sin…

Models MolecularPhotoisomerizationNitrogenSurface PropertiesQuantum yieldCrystallography X-RayLigandsProtein EngineeringPhotochemistryBiochemistrychemistry.chemical_compoundparasitic diseasesSide chainAnimalsCloning MolecularneoplasmsMolecular BiologySpectroscopy Near-InfraredBiliverdinBacteriaPhytochromeChemistryBiliverdinetechnology industry and agricultureta1182WaterHydrogen BondingCell BiologyChromophoreequipment and suppliesFluorescenceProtein Structure Tertiarysurgical procedures operativeSpectrometry FluorescenceStructural biologySpectrophotometryProtein Structure and FoldingPhytochromeHydrophobic and Hydrophilic InteractionsBiomarkersProtein BindingJournal of Biological Chemistry
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Interfacial behavior of recombinant forms of human pulmonary surfactant protein SP-C.

2012

The behavior at air-liquid interfaces of two recombinant versions of human surfactant protein SP-C has been characterized in comparison with that of native palmitoylated SP-C purified from porcine lungs. Both native and recombinant proteins promoted interfacial adsorption of dipalmitoylphosphatidylcholine bilayers to a limited extent, but catalyzed very rapid formation of films from different lipid mixtures containing both zwitterionic and anionic phospholipids. Once at the interface, the recombinant variants exhibited compression-driven structural transitions, consistent with changes in the orientation of the deacylated N-terminal segment, which were not observed in the native protein. Com…

Models MolecularProtein ConformationSurface PropertiesMolecular Sequence DataCatalysislaw.inventionchemistry.chemical_compoundAdsorptionPulmonary surfactantlawMoleElectrochemistryMoleculeNative proteinAnimalsHumansGeneral Materials ScienceAmino Acid SequenceSpectroscopyPhospholipidsSurfaces and InterfacesCondensed Matter PhysicsPulmonary Surfactant-Associated Protein CPeptide FragmentsRecombinant ProteinschemistryBiochemistryDipalmitoylphosphatidylcholineRecombinant DNABiophysicsLangmuir : the ACS journal of surfaces and colloids
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The amorphous silica-liquid water interface studied by ab initio molecular dynamics (AIMD): local organization in global disorder

2014

International audience; The structural organization of water at a model of amorphous silica-liquid water interface is investigated by ab initio molecular dynamics (AIMD) simulations at room temperature. The amorphous surface is constructed with isolated, H-bonded vicinal and geminal silanols. In the absence of water, the silanols have orientations that depend on the local surface topology (i.e. presence of concave and convex zones). However, in the presence of liquid water, only the strong inter-silanol H-bonds are maintained, whereas the weaker ones are replaced by H-bonds formed with interfacial water molecules. All silanols are found to act as H- bond donors to water. The vicinal silanol…

Models MolecularProtonSurface Propertiesamorphous silicawatergeminal silanols02 engineering and technologyMolecular Dynamics Simulation010402 general chemistry01 natural sciencesAb initio molecular dynamicsComputational chemistryMoleculeGeneral Materials ScienceQuartzGeminalMolecular StructureChemistryab initio molecular dynamicsHydrogen Bonding[CHIM.MATE]Chemical Sciences/Material chemistrySilanes021001 nanoscience & nanotechnologyCondensed Matter PhysicsSilicon Dioxide0104 chemical sciencesAmorphous solidChemical physicsQuantum TheoryAmorphous silicaProtons0210 nano-technologyVicinal
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Structural Characterization of Set1 RNA Recognition Motifs and their Role in Histone H3 Lysine 4 Methylation

2006

Departament de Bioquimica iBiologia Molecular, Universitatde Valencia, C/Dr Moliner 50,46100, Burjassot, SpainThe yeast Set1 histone H3 lysine 4 (H3K4) methyltransferase contains, inaddition to its catalytic SET domain, a conserved RNA recognition motif(RRM1). We present here the crystal structure and the secondary structureassignment in solution of the Set1 RRM1. Although RRM1 has the expectedβαββαβ RRM-fold, it lacks the typical RNA-binding features of thesemodules. RRM1 is not able to bind RNA by itself in vitro, but a constructcombining RRM1 with a newly identified downstream RRM2 specificallybinds RNA. Invivo,H3K4 methylation isnot affectedbyapoint mutation inRRM2 that preserves Set1 s…

Models MolecularRiboswitchHistone H3 Lysine 4Saccharomyces cerevisiae ProteinsRNA-induced transcriptional silencingSurface Properties[SDV]Life Sciences [q-bio]Molecular Sequence DataSaccharomyces cerevisiae[SDV.BC.BC]Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC]BiologyMethylationHistonesStructure-Activity Relationship03 medical and health sciencesStructural BiologyHistone methylation[SDV.BC.BC] Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC]Amino Acid SequenceProtein Structure QuaternaryMolecular BiologyConserved Sequence030304 developmental biology0303 health sciencesRNA recognition motifLysine030302 biochemistry & molecular biologyRNARNA FungalHistone-Lysine N-MethyltransferaseNon-coding RNAMolecular biology[SDV] Life Sciences [q-bio]DNA-Binding ProteinsProtein SubunitsBiochemistryHistone methyltransferaseSequence AlignmentProtein BindingTranscription Factors
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