Search results for " microscopy"

showing 10 items of 1617 documents

Au-40(SR)(24) Cluster as a Chiral Dimer of 8-Electron Superatoms: Structure and Optical Properties

2012

We predict and analyze density-functional theory (DFT)-based structures for the recently isolated Au(40)(SR)(24) cluster. Combining structural information extracted from ligand-exchange reactions, circular dichroism and transmission electron microscopy leads us to propose two families of low-energy structures that have a chiral Au-S framework on the surface. These families have a common geometrical motif where a nonchiral Au(26) bi-icosahedral cluster core is protected by 6 RS-Au-SR and 4 RS-Au-SR-Au-SR oligomeric units, analogously to the "Divide and Protect" motif of known clusters Au(25)(SR)(18)(-/0), Au(38)(SR)(24) and Au(102)(SR)(44). The strongly prolate shape of the proposed Au(26) c…

Models MolecularCircular dichroismIcosahedral symmetryDimerShell (structure)Electrons02 engineering and technologyElectronElectronic structure010402 general chemistry01 natural sciencesBiochemistryCatalysischemistry.chemical_compoundColloid and Surface ChemistryCluster (physics)ta114ChemistryCircular DichroismStereoisomerismGeneral Chemistry021001 nanoscience & nanotechnology0104 chemical sciencesCrystallographyTransmission electron microscopyddc:540Quantum Theory0210 nano-technologyDimerizationOrganogold CompoundsJournal of the American Chemical Society
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Self-assembly of janus dendrimers into uniform dendrimersomes and other complex architectures

2010

Janus Drug Delivery Vehicle Efficient drug delivery vehicles need to be produced in a limited size range and with uniform size distribution. The self-assembly of traditional small-molecule and polymeric amphiphiles has led to the production of micelles, liposomes, polymeric micelles, and polymersomes for use in drug delivery applications. Now, Percec et al. (p. 1009 ) describe the self-assembly of Janus-type (i.e., two-headed) dendrimers to produce monodisperse supramolecular constructs, termed “dendrimersomes,” and other complex architectures. The structures, which showed long-term stability as well as very narrow size distributions, were easily produced by the injection of an ethanolic so…

Models MolecularDendrimersMaterials scienceSurface Propertiesta221Complex ArchitecturesNanotechnologyMolecular Dynamics SimulationSurface-Active AgentsBiomimetic MaterialsDendrimerAmphiphileJanusta218LiposomeDrug Carriersta214MultidisciplinaryAntibiotics Antineoplasticta114Molecular StructureVesicleCryoelectron MicroscopyWaterMembranes ArtificialNanostructuresJanus DendrimersSelf-AssemblyMembraneUniform DendrimersomesDoxorubicinPolymersomeSelf-assemblyHydrophobic and Hydrophilic InteractionsScience
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Extracellular Albumin and Endosomal Ions Prime Enterovirus Particles for Uncoating That Can Be Prevented by Fatty Acid Saturation

2019

ABSTRACT There is limited information about the molecular triggers leading to the uncoating of enteroviruses under physiological conditions. Using real-time spectroscopy and sucrose gradients with radioactively labeled virus, we show at 37°C, the formation of albumin-triggered, metastable uncoating intermediate of echovirus 1 without receptor engagement. This conversion was blocked by saturating the albumin with fatty acids. High potassium but low sodium and calcium concentrations, mimicking the endosomal environment, also induced the formation of a metastable uncoating intermediate of echovirus 1. Together, these factors boosted the formation of the uncoating intermediate, and the infectiv…

Models MolecularEchovirusHot TemperatureEndosomevirusesImmunologycryoEM structurerasvahapotEndosomesBiologymedicine.disease_causeMicrobiologyDivalentCell Line03 medical and health sciencesVirologyAlbuminsChlorocebus aethiopsExtracellularmedicineAnimalsalbumin030304 developmental biologychemistry.chemical_classificationalbumiinit0303 health sciencesbiokemiaionitenterovirus030302 biochemistry & molecular biologyCryoelectron MicroscopyFatty AcidsFatty acidRNAVirus-Cell InteractionsEnterovirus B HumanenteroviruksetchemistryCapsidvirologia13. Climate actionInsect ScienceBiophysicsCapsid ProteinsuncoatingLow sodium
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Electron Microscopy of Human Erythrocyte Catalase: New Two-Dimensional Crystal Forms

1993

Abstract Using the mica-spreading "negative staining-carbon film" procedure, human erythrocyte catalase has been shown to create a number of different periodic or crystalline two-dimensional (2-D) arrays which differ in the arrangement of molecules in the repeating units and the lattice type. Digital image processing has been performed with a 2-D array which contains regularly arranged "undulating" rows of molecules and also with a 2-D crystal form, exhibiting pgg (p22 1 2 1 ) symmetry and lattice parameters of a = 12.7 nm, b = 44 nm, and γ= 92°. The data are compared with our previous analysis of a different human erythrocyte catalase 2-D crystal, and the effect of partial-depth negative s…

Models MolecularErythrocytesFourier AnalysisbiologyMolecular modelProtein ConformationChemistryStereochemistryCatalaseNegative stainlaw.inventionCrystalMicroscopy ElectronCrystallographyStructural BiologyCatalaseTransmission electron microscopylawLattice (order)biology.proteinHumansMoleculeComputer SimulationElectron microscopeJournal of Structural Biology
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Evolution of molluscan hemocyanin structures

2013

AbstractHemocyanin transports oxygen in the hemolymph of many molluscs and arthropods and is therefore a central physiological factor in these animals. Molluscan hemocyanin molecules are oligomers composed of many protein subunits that in turn encompass subsets of distinct functional units. The structure and evolution of molluscan hemocyanin have been studied for decades, but it required the recent progress in DNA sequencing, X-ray crystallography and 3D electron microscopy to produce a detailed view of their structure and evolution. The basic quaternary structure is a cylindrical decamer 35nm in diameter, consisting of wall and collar (typically at one end of the cylinder). Depending on th…

Models MolecularEvolutionProtein Conformationmedicine.medical_treatmentProtein subunitProtein Data Bank (RCSB PDB)BiophysicsCrystallography X-RayHemocyaninBiochemistryAnalytical ChemistryRespiratory proteinsPaleontologyHemolymphElectron microscopymedicineQuaternary structureAnimalsMolecular BiologybiologyHemocyanincomputer.file_formatKeyhole limpet hemocyaninProtein Data BankBiological EvolutionMolluscaEvolutionary biologyHemocyaninsbiology.proteinProtein quaternary structureKLHcomputerKeyhole limpet hemocyaninOxygen bindingBiochimica et Biophysica Acta (BBA) - Proteins and Proteomics
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Subphthalocyanines: addressing water-solubility, nano-encapsulation, and activation for optical imaging of B16 melanoma cells

2014

Water-soluble disulfonato-subphthalocyanines (SubPcs) or hydrophobic nano-encapsulated SubPcs are efficient probes for the fluorescence imaging of cells. 20 nm large liposomes (TEM and DLS) incorporated about 13% SubPc. Moreover, some of these fluorophores were found to be pH activatable.

Models MolecularFluorescence-lifetime imaging microscopyNanostructureIndolesMelanoma ExperimentalIsoindoles010402 general chemistryPhotochemistryCrystallography X-Ray01 natural sciencesCatalysisMiceMaterials ChemistryMoleculeAnimals[CHIM]Chemical SciencesSolubilityFluorescent DyesLiposomeAqueous solutionMolecular Structure010405 organic chemistryChemistryMetals and AlloysWaterGeneral ChemistryHydrogen-Ion Concentration0104 chemical sciencesSurfaces Coatings and FilmsElectronic Optical and Magnetic MaterialsMolecular ImagingNanostructuresNano encapsulationSolubilityLiposomesCeramics and CompositesMolecular imaging
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Finely Tuned Temperature-Controlled Cargo Release Using Paraffin-Capped Mesoporous Silica Nanoparticles

2011

[EN] Trapped: Mesoporous silica nanoparticles were loaded with a fluorescent guest and functionalized with octadecyltrimethoxysilane. The alkyl chains interact with paraffins, which build a hydrophobic layer around the particle (see picture). Upon melting of the paraffin, the guest molecule is released, as demonstrated in cells for the guest doxorubicin. The release temperature can be tuned by choosing an appropriate paraffin. Copyright © 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

Models MolecularINGENIERIA DE LA CONSTRUCCIONGuest moleculesParaffinsParaffin waxesNanoparticlemesoporous materialsMCM-41Phenazine derivativeFunctionalizedCell survivalNanoparticleQUIMICA ORGANICAChemical structureX-Ray DiffractionSafranin tSilicon dioxideControlled releaseAlkyl chainDrug CarriersMicroscopy ConfocalMolecular StructureOctadecyltrimethoxysilaneSurface propertyTemperatureSilicaGeneral MedicineChemistryAntineoplastic agentParaffinHeLa cellPorosityHumanMaterials scienceDrug carrierX ray diffractionSurface PropertiesMesoporous silica nanoparticlesNanotechnologyAntineoplastic AgentsMesoporousCatalysisDrug interactionsArticleMicroscopy Electron TransmissionHumansCell survivalDrug effectDelayed release formulationHydrophobic layersQUIMICA INORGANICAGeneral ChemistryMesoporous silicaMolecular gatesMesoporous materialsMcm 41Confocal microscopyDrug effectSolubilityDoxorubicinDelayed-Action Preparationsdrug deliveryDrug deliveryNanoparticlesPhenazinesnanoparticlesMesoporous materialcontrolled releasemolecular gatesTransmission electron microscopyHeLa CellsAngewandte Chemie
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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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Impact of local compressive stress on the optical transitions of single organic dye molecules

2012

The ability to mechanically control the optical properties of individual molecules is a grand challenge in nanoscience and could enable the manipulation of chemical reactivity at the single-molecule level. In the past, light has been used to alter the emission wavelength of individual molecules or modulate the energy transfer quantum yield between them. Furthermore, tensile stress has been applied to study the force dependence of protein folding/unfolding and of the chemistry and photochemistry of single molecules, although in these mechanical experiments the strength of the weakest bond limits the amount of applicable force. Here, we show that compressive stress modifies the photophysical …

Models MolecularMaterials scienceBiomedical EngineeringBioengineeringNanotechnologyImidesMicroscopy Atomic ForceMolecular physicslaw.inventionAdsorptionConfocal microscopylawMoleculeGeneral Materials ScienceEmission spectrumPhysics::Chemical PhysicsElectrical and Electronic EngineeringColoring AgentsPeryleneAtomic force microscopyEquipment DesignCondensed Matter PhysicsAtomic and Molecular Physics and OpticsCompressive strengthEnergy TransferMicroscopy FluorescenceOrganic dyeStress MechanicalNature Nanotechnology
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Limulus polyphemus Hemocyanin: 10 Å Cryo-EM Structure, Sequence Analysis, Molecular Modelling and Rigid-body Fitting Reveal the Interfaces Between th…

2007

Abstract The blue copper protein hemocyanin from the horseshoe crab Limulus polyphemus is among the largest respiratory proteins found in nature (3.5 MDa) and exhibits a highly cooperative oxygen binding. Its 48 subunits are arranged as eight hexamers (1×6mers) that form the native 8×6mer in a nested hierarchy of 2×6mers and 4×6mers. This quaternary structure is established by eight subunit types (termed I, IIA, II, IIIA, IIIB, IV, V, and VI), of which only type II has been sequenced. Crystal structures of the 1×6mer are available, but for the 8×6mer only a 40 A 3D reconstruction exists. Consequently, the structural parameters of the 8×6mer are not firmly established, and the molecular inte…

Models MolecularMolecular modelCryo-electron microscopyCopper proteinProtein subunitmedicine.medical_treatmentMolecular Sequence DataStructure-Activity RelationshipStructural BiologyHorseshoe CrabsmedicineAnimalsAmino Acid SequenceProtein Structure QuaternaryMolecular BiologyPhylogenySequence Homology Amino AcidbiologyCryoelectron MicroscopyHemocyaninbiology.organism_classificationProtein Structure TertiaryCrystallographyLimulusHemocyaninsProtein quaternary structureOxygen bindingJournal of Molecular Biology
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