Search results for "Interactions"

showing 10 items of 1963 documents

Backbone dynamics of rusticyanin: the high hydrophobicity and rigidity of this blue copper protein is responsible for its thermodynamic properties.

2003

Local dynamics and solute-solvent exchange properties of rusticyanin (Rc) from Thiobacillus ferrooxidans have been studied by applying heteronuclear ((1)H, (15)N) NMR spectroscopy. (15)N relaxation parameters have been determined for the reduced protein, and a model-free analysis has been applied. The high average value of the generalized order parameter, S(2) (0.93), indicates that Rc is very rigid. The analysis of cross correlation rates recorded in both the reduced and the oxidized forms conclusively proves that Rc possesses the same dynamic features in both oxidation states. The accessibility of backbone amide protons to the solvent at different time scales has also been studied by appl…

Models MolecularMagnetic Resonance SpectroscopyCopper proteinWaterNuclear magnetic resonance spectroscopyThiobacillusBiochemistryProtein Structure SecondaryProtein Structure TertiarySolventMetalchemistry.chemical_compoundCrystallographyProtein structureHeteronuclear moleculechemistryBacterial ProteinsAzurinvisual_artAmideRusticyaninvisual_art.visual_art_mediumThermodynamicsHydrophobic and Hydrophilic InteractionsCopperBiochemistry
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Mapping the fluorophilicity of a hydrophobic pocket: synthesis and biological evaluation of tricyclic thrombin inhibitors directing fluorinated alkyl…

2006

In the completion of our fluorine scan of tricyclic inhibitors to map the fluorophilicity/fluorophobicity of the thrombin active site, a series of 11 new ligands featuring alkyl, alkenyl, and fluoroalkyl groups was prepared to explore fluorine effects on binding into the hydrophobic proximal (P) pocket, lined by Tyr 60A and Trp 60D, His 57, and Leu 99. The synthesis of the tricyclic scaffolds was based on the 1,3-dipolar cycloaddition of azomethine ylides, derived from L-proline and 4-bromobenzaldehyde, with N-(4-fluorobenzyl)maleimide. Introduction of alkyl, alkenyl, and partially fluorinated alkyl residues was achieved upon substitution of a sulfonyl group by mixed Mg/Zn organometallics f…

Models MolecularMagnetic Resonance SpectroscopySpectrophotometry InfraredStereochemistrySubstituentCrystallography X-RayBiochemistryAntithrombinschemistry.chemical_compoundDrug DiscoveryNon-covalent interactionsGeneral Pharmacology Toxicology and PharmaceuticsMaleimideAlkylPharmacologychemistry.chemical_classificationSulfonylNucleophilic additionbiologyMolecular StructureOrganic ChemistryActive siteFluorineCycloadditionchemistrySpectrometry Mass Matrix-Assisted Laser Desorption-Ionizationbiology.proteinMolecular MedicineChemMedChem
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A Fluorine Scan at the Catalytic Center of Thrombin: CF, COH, and COMe Bioisosterism and Fluorine Effects on pKa and logD Values

2006

A series of 16 tricyclic thrombin inhibitors was prepared by using the 1,3-dipolar cycloaddition of azomethine ylides derived from 3- or 4-hydroxyproline and 4-bromobenzaldehyde, with N-(4-fluorobenzyl)maleimide as the key step. The terminal pyrrolidine ring of the inhibitors was systematically substituted to explore the potential bioisosteric behavior of C-F, C-OH, and C-OMe residues pointing into the environment of the catalytic center of a serine protease. X-ray crystal structure analyses revealed a distinct puckering preference of this ring. Substitution by F, HO, and MeO has a strong effect on the basicity of the adjacent pyrrolidine nitrogen center which originates from two sigma-indu…

Models MolecularMagnetic Resonance SpectroscopyTertiary amineStereochemistrychemistry.chemical_elementCrystal structureBiochemistryPyrrolidinechemistry.chemical_compoundCatalytic DomainDrug DiscoveryNon-covalent interactionsGeneral Pharmacology Toxicology and PharmaceuticsMaleimidePharmacologychemistry.chemical_classificationMolecular StructureOrganic ChemistryThrombinFluorineAcceptorCycloadditionchemistrySpectrometry Mass Matrix-Assisted Laser Desorption-IonizationFluorineMolecular MedicineChemMedChem
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Tuning molecular self-assembly on bulk insulator surfaces by anchoring of the organic building blocks.

2013

Molecular self-assembly constitutes a versatile strategy for creating functional structures on surfaces. Tuning the subtle balance between intermolecular and molecule-surface interactions allows structure formation to be tailored at the single-molecule level. While metal surfaces usually exhibit interaction strengths in an energy range that favors molecular self-assembly, dielectric surfaces having low surface energies often lack sufficient interactions with adsorbed molecules. As a consequence, application-relevant, bulk insulating materials pose significant challenges when considering them as supporting substrates for molecular self-assembly. Here, the current status of molecular self-ass…

Models MolecularMaterials scienceAnchoringNanotechnologyInsulator (electricity)Dielectricmolecular adsorption530Molecular self-assemblyMoleculeGeneral Materials ScienceComputer Simulationnon-contact atomic forceOrganic Chemicalsinsulating surfacesMechanical EngineeringIntermolecular forceElectric Conductivityself-assemblymolecule-surface interactionsModels ChemicalMechanics of MaterialsMetalsmicroscopySelf-assemblyNon-contact atomic force microscopyAdvanced materials (Deerfield Beach, Fla.)
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Cationic Nanohydrogel Particles as Potential siRNA Carriers for Cellular Delivery

2012

Oligonucleotides such as short, double-stranded RNA (siRNA) or plasmid DNA (pDNA) promise high potential in gene therapy. For pharmaceutical application, however, adequate drug carriers are required. Among various concepts progressing in the market or final development, nanosized hydrogel particles may serve as novel transport media especially for siRNA. In this work, a new concept of synthesizing polymeric cationic nanohydrogels was developed, which offers a promising strategy to complex and transport siRNA into cells. For this purpose, amphiphilic reactive ester block copolymers were synthesized by RAFT polymerization of pentafluorophenyl methacrylate as reactive ester monomer together wi…

Models MolecularMaterials scienceMolecular ConformationGeneral Physics and AstronomyMethacrylateCell Linechemistry.chemical_compoundAmphiphilePolymer chemistryAnimalsGeneral Materials ScienceReversible addition−fragmentation chain-transfer polymerizationAminesRNA Small Interferingchemistry.chemical_classificationDrug CarriersGeneral EngineeringCationic polymerizationBiological TransportEstersHydrogelsPolymerCombinatorial chemistryNanostructuresRatsMonomerchemistrySolventsDrug carrierHydrophobic and Hydrophilic InteractionsEthylene glycolACS Nano
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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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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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Lhca5 interaction with plant photosystem I

2006

AbstractIn the outer antenna (LHCI) of higher plant photosystem I (PSI) four abundantly expressed light-harvesting protein of photosystem I (Lhca)-type proteins are organized in two heterodimeric domains (Lhca1/Lhca4 and Lhca2/Lhca3). Our cross-linking studies on PSI-LHCI preparations from wildtype Arabidopsis and pea plants indicate an exclusive interaction of the rarely expressed Lhca5 light-harvesting protein with LHCI in the Lhca2/Lhca3-site. In PSI particles with an altered LHCI composition Lhca5 assembles in the Lhca1/Lhca4 site, partly as a homodimer. This flexibility indicates a binding-competitive model for the LHCI assembly in plants regulated by molecular interactions of the Lhca…

Models MolecularPhotosystem IArabidopsisLight-Harvesting Protein ComplexesBiophysicsPhotosystem IBiochemistrychemistry.chemical_compoundLight harvesting complex IStructural BiologyArabidopsisGeneticsMolecular BiologyLhca5Molecular interactionsPhotosystem I Protein ComplexbiologyArabidopsis ProteinsPeasWild typefood and beveragesArabidopsis ProteinsCell BiologyLight-Harvesting Protein Complexesbiology.organism_classificationCrystallographychemistryChlorophyllBiophysicsLight-harvesting complex ICross-linkingFEBS Letters
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Mediation of Elicitin Activity on Tobacco Is Assumed by Elicitin-Sterol Complexes

2001

Elicitins secreted by phytopathogenic Phytophthora spp. are proteinaceous elicitors of plant defense mechanisms and were demonstrated to load, carry, and transfer sterols between membranes. The link between elicitor and sterol-loading properties was assessed with the use of site-directed mutagenesis of the 47 and 87 cryptogein tyrosine residues, postulated to be involved in sterol binding. Mutated cryptogeins were tested for their ability to load sterols, bind to plasma membrane putative receptors, and trigger biological responses. For each mutated elicitin, the chemical characterization of the corresponding complexes with stigmasterol (1:1 stoichiometry) demonstrated their full functionali…

Models MolecularPhytophthora0106 biological sciencesTime FactorsProtein Conformation[SDV]Life Sciences [q-bio]Receptors Cell SurfaceBiologyModels Biological01 natural sciencesArticleHost-Parasite InteractionsFungal Proteins03 medical and health sciencesTobaccoProtein IsoformsBinding siteReceptorMolecular BiologyComputingMilieux_MISCELLANEOUSCells CulturedPlant DiseasesPlant Proteins030304 developmental biology0303 health sciencesBinding SitesAlgal ProteinsCell MembraneProteinsElicitinCell BiologyHydrogen-Ion ConcentrationLigand (biochemistry)Receptor–ligand kineticsSterolElicitor[SDV] Life Sciences [q-bio]SterolsBiochemistryTyrosineCalciumSterol bindingProtein Binding010606 plant biology & botanyMolecular Biology of the Cell
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Biomimetic oxygen reduction by cofacial porphyrins at a liquid-liquid interface.

2012

Oxygen reduction catalyzed by cofacial metalloporphyrins at the 1,2-dichlorobenzene−water interface was studied with two lipophilic electron donors of similar driving force, 1,1'-dimethylferrocene (DMFc) and tetrathiafulvalene (TTF). The reaction produces mainly water and some hydrogen peroxide, but the mediator has a significant effect on the selectivity, as DMFc and the porphyrins themselves catalyze the decomposition and the further reduction of hydrogen peroxide. Density functional theory calculations indicate that the biscobaltporphyr- in, 4,5-bis(5-(2,8,13,17-tetraethyl-3,7,12,18-tetramethylporphyrinyl))-9,9-dimethylxanthene, Co2(DPX), actually catalyzes oxygen reduction to hydrogen p…

Models MolecularPorphyrinsMolecular Conformationchemistry.chemical_element02 engineering and technology010402 general chemistryPhotochemistry01 natural sciencesBiochemistryOxygenCatalysisCatalysisElectron Transportchemistry.chemical_compoundColloid and Surface ChemistryBiomimeticsHeterocyclic CompoundsMoleculePerchloric acidFerrous CompoundsHydrogen peroxideta116ElectrodesSelective catalytic reductionGeneral Chemistry021001 nanoscience & nanotechnology0104 chemical sciencesOxygenchemistryQuantum Theory0210 nano-technologySelectivityHydrophobic and Hydrophilic InteractionsTetrathiafulvaleneJournal of the American Chemical Society
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