Search results for "photobleaching"

showing 10 items of 59 documents

Energy Transfer between Surface-Immobilized Light-Harvesting Chlorophyll a/b Complex (LHCII) Studied by Surface Plasmon Field-Enhanced Fluorescence S…

2010

The major light-harvesting chlorophyll a/b complex (LHCII) of the photosynthetic apparatus in green plants can be viewed as a protein scaffold binding and positioning a large number of pigment molecules that combines rapid and efficient excitation energy transfer with effective protection of its pigments from photobleaching. These properties make LHCII potentially interesting as a light harvester (or a model thereof) in photoelectronic applications. Most of such applications would require the LHCII to be immobilized on a solid surface. In a previous study we showed the immobilization of recombinant LHCII on functionalized gold surfaces via a 6-histidine tag (His tag) in the protein moiety. …

Models MolecularChlorophyll aProtein ConformationSurface PropertiesLight-Harvesting Protein ComplexesPhotochemistryFluorescence spectroscopyAbsorptionchemistry.chemical_compoundFluorescence Resonance Energy TransferElectrochemistryMoleculeGeneral Materials ScienceSpectroscopyFluorescent DyesSurface plasmonPeasSurfaces and InterfacesEnzymes ImmobilizedCondensed Matter PhysicsPhotobleachingFluorescenceAcceptorKineticsB vitaminschemistryLangmuir
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Effect of ATP Binding and Hydrolysis on Dynamics of Canine Parvovirus NS1▿ †

2010

ABSTRACT The replication protein NS1 is essential for genome replication and protein production in parvoviral infection. Many of its functions, including recognition and site-specific nicking of the viral genome, helicase activity, and transactivation of the viral capsid promoter, are dependent on ATP. An ATP-binding pocket resides in the middle of the modular NS1 protein in a superfamily 3 helicase domain. Here we have identified key ATP-binding amino acid residues in canine parvovirus (CPV) NS1 protein and mutated amino acids from the conserved A motif (K406), B motif (E444 and E445), and positively charged region (R508 and R510). All mutations prevented the formation of infectious viruse…

Models MolecularParvovirus CaninevirusesImmunologyMolecular Sequence DataPlasma protein bindingViral Nonstructural ProteinsMicrobiologyCell Linechemistry.chemical_compoundAdenosine TriphosphateDogsVirologyAnimalsAmino Acid SequenceBinding siteBinding SitesbiologyHydrolysisDNA replicationHelicaseFluorescence recovery after photobleachingFusion proteinMolecular biologyGenome Replication and Regulation of Viral Gene ExpressionProtein Structure TertiaryViral replicationchemistryBiochemistryAmino Acid SubstitutionInsect Sciencebiology.proteinCatsMutagenesis Site-DirectedSequence AlignmentDNAProtein Binding
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Distribution and Dynamics of Transcription-Associated Proteins during Parvovirus Infection

2012

ABSTRACT Canine parvovirus (CPV) infection leads to reorganization of nuclear proteinaceous subcompartments. Our studies showed that virus infection causes a time-dependent increase in the amount of viral nonstructural protein NS1 mRNA. Fluorescence recovery after photobleaching showed that the recovery kinetics of nuclear transcription-associated proteins, TATA binding protein (TBP), transcription factor IIB (TFIIB), and poly(A) binding protein nuclear 1 (PABPN1) were different in infected and noninfected cells, pointing to virus-induced alterations in binding dynamics of these proteins.

Parvovirus CanineViral nonstructural proteinvirusesImmunologyMicrobiologyParvoviridae Infections03 medical and health sciencesVirologyAnimalsTranscription factor030304 developmental biology0303 health sciencesbiologyParvovirusBinding protein030302 biochemistry & molecular biologyCanine parvovirusFluorescence recovery after photobleachingbiology.organism_classificationMolecular biology3. Good healthVirus-Cell InteractionsCell CompartmentationInsect Sciencebiology.proteinTATA-binding proteinTranscription factor II BSubcellular FractionsTranscription Factors
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Parvovirus induced alterations in nuclear architecture and dynamics.

2009

The nucleus of interphase eukaryotic cell is a highly compartmentalized structure containing the three-dimensional network of chromatin and numerous proteinaceous subcompartments. DNA viruses induce profound changes in the intranuclear structures of their host cells. We are applying a combination of confocal imaging including photobleaching microscopy and computational methods to analyze the modifications of nuclear architecture and dynamics in parvovirus infected cells. Upon canine parvovirus infection, expansion of the viral replication compartment is accompanied by chromatin marginalization to the vicinity of the nuclear membrane. Dextran microinjection and fluorescence recovery after ph…

Parvovirus CaninevirusesGreen Fluorescent Proteinslcsh:MedicineGenome ViralKidneyParvoviridae InfectionsParvovirus03 medical and health sciencesLääketieteen bioteknologia - Medical biotechnologymedicineAnimalsHumansNuclear membraneMolecular Biology/Chromatin Structurelcsh:Science030304 developmental biologyMolecular Biology/DNA ReplicationCell Nucleus0303 health sciencesMultidisciplinaryMicroscopy ConfocalbiologyParvoviruslcsh:R030302 biochemistry & molecular biologyDNA replicationFluorescence recovery after photobleachingDextransbiology.organism_classificationMolecular biologyChromatin3. Good healthChromatinCell biologyCell nucleusmedicine.anatomical_structureViral replicationVirology/Viral Replication and Gene RegulationCatslcsh:QCell Biology/Nuclear Structure and FunctionViral genome replicationFluorescence Recovery After PhotobleachingHeLa CellsResearch ArticlePloS one
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Demonstration of Single-Barium-Ion Sensitivity for Neutrinoless Double-Beta Decay Using Single-Molecule Fluorescence Imaging

2018

[EN] A new method to tag the barium daughter in the double-beta decay of Xe-136 is reported. Using the technique of single molecule fluorescent imaging (SMFI), individual barium dication (Ba++) resolution at a transparent scanning surface is demonstrated. A single-step photobleach confirms the single ion interpretation. Individual ions are localized with superresolution (similar to 2 nm), and detected with a statistical significance of 12.9 sigma over backgrounds. This lays the foundation for a new and potentially background-free neutrinoless double-beta decay technology, based on SMFI coupled to high pressure xenon gas time projection chambers.

Physics - Instrumentation and DetectorsMaterials scienceMassesFOS: Physical sciencesGeneral Physics and Astronomychemistry.chemical_element01 natural sciences7. Clean energyMolecular physicsHigh Energy Physics - ExperimentIonTECNOLOGIA ELECTRONICAHigh Energy Physics - Experiment (hep-ex)Nuclear magnetic resonanceXenonDouble beta decay0103 physical sciencesNuclear Experiment (nucl-ex)010306 general physicsNuclear Experiment010308 nuclear & particles physicsBariumInstrumentation and Detectors (physics.ins-det)Single-molecule experimentPhotobleachingFluorescenceDicationchemistry
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Control of the electronic energy transfer pathway between two single fluorophores by dual pulse excitation.

2009

We report on the control of the energy transfer pathway in individual donor-acceptor dyads by proper timing of light pulses matching the donor and acceptor transition frequencies, respectively. Excitation of both chromophores at virtually the same time induces efficient singlet-singlet annihilation, whereby excitation energy effectively flows from the acceptor to the donor. The dual pulse excitation scheme implemented here allows for all-optical switching of the fluorescence intensity at the single-molecule level. The population of higher excited states at the donor site was found to significantly increase the photobleaching probability.

Physics::Biological Physicseducation.field_of_studyMaterials sciencePopulationGeneral Physics and AstronomyP680ChromophorePhotobleachingAcceptorCondensed Matter::Materials ScienceFörster resonance energy transferExcited statePhysics::Chemical PhysicsAtomic physicseducationExcitationPhysical review letters
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Modification of Plasma Membrane Organization in Tobacco Cells Elicited by Cryptogein

2014

Abstract Lipid mixtures within artificial membranes undergo a separation into liquid-disordered and liquid-ordered phases. However, the existence of this segregation into microscopic liquid-ordered phases has been difficult to prove in living cells, and the precise organization of the plasma membrane into such phases has not been elucidated in plant cells. We developed a multispectral confocal microscopy approach to generate ratiometric images of the plasma membrane surface of Bright Yellow 2 tobacco (Nicotiana tabacum) suspension cells labeled with an environment sensitive fluorescent probe. This allowed the in vivo characterization of the global level of order of this membrane, by which w…

Physiology[SDV]Life Sciences [q-bio]BiophysicsContext (language use)Pyridinium CompoundsPlant ScienceBiologyArticleFungal ProteinsTobaccoGeneticsMembrane fluidity[SDV.BV]Life Sciences [q-bio]/Vegetal BiologyFluorescent DyesPlasma membrane organizationChromatographyMicroscopy ConfocalPhotobleachingCell MembraneFluorescence recovery after photobleachingMembrane raftfood and beveragesPlant cellElicitorSterolsMembrane[SDE]Environmental SciencesBiophysicsFlagellinSignal Transduction
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Functional size of complement and perforin pores compared by confocal laser scanning microscopy and fluorescence microphotolysis

1991

Abstract Confocal laser scanning microscopy and fluorescence microphotolysis (also referred to as fluorescence photobleaching recovery) were employed to study the transport of hydrophilic fluorescent tracers through complement and perforin pores. By optimizing the confocal effect it was possible to determine the exclusion limit of the pores in situ, i.e. without separation of cells and tracer solution. Single-cell flux measurements by fluorescence microphotolysis yielded information on the sample population distribution of flux rates. By these means a direct comparison of complement and perforin pores was made in sheep erythrocyte membranes. In accordance with previous studies employing a v…

Pore Forming Cytotoxic ProteinsIn situCell Membrane PermeabilityConfocalBiophysicsAntigen-Antibody ComplexIn Vitro TechniquesBiologyBiochemistryTumor Cells CulturedmedicineAnimalsHumansMembrane GlycoproteinsSheepPerforinLasersCell MembraneErythrocyte MembraneMembrane ProteinsComplement System ProteinsCell BiologyFluorescencePhotobleachingCell biologyRed blood cellmedicine.anatomical_structureMembranePerforinMicroscopy Electron Scanningbiology.proteinCytolysinBiochimica et Biophysica Acta (BBA) - Biomembranes
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Autofluorescence imaging of basal cell carcinoma by smartphone RGB camera

2015

The feasibility of smartphones for in vivo skin autofluorescence imaging has been investigated. Filtered autofluorescence images from the same tissue area were periodically captured by a smartphone RGB camera with subsequent detection of fluorescence intensity decreasing at each image pixel for further imaging the planar distribution of those values. The proposed methodology was tested clinically with 13 basal cell carcinoma and 1 atypical nevus. Several clinical cases and potential future applications of the smartphone-based technique are discussed.

PorphyrinsSkin NeoplasmsLightComputer scienceBiomedical EngineeringDermoscopyImage processingFluorescenceBiomaterialsOpticsmedicineHumansBasal cell carcinomaNevusSkinPhotobleachingPixelbusiness.industrySkin autofluorescenceNADmedicine.diseaseAtypical nevusAtomic and Molecular Physics and OpticsElectronic Optical and Magnetic MaterialsAutofluorescenceFluorescence intensityMicroscopy FluorescenceCarcinoma Basal CellRGB color modelCollagenSmartphonebusinessBiomedical engineeringJournal of Biomedical Optics
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Thioflavin T templates amyloid β(1–40) conformation and aggregation pathway

2015

Aβ(1-40) peptide supramolecular assembly and fibril formation processes are widely recognized to have direct implications in the progression of Alzheimer's disease. The molecular basis of this biological process is still unknown and there is a strong need of developing effective strategies to control the occurring events. To this purpose the exploitation of small molecules interacting with Aβ aggregation represents one of the possible routes. Moreover, the use specific labeling has represented so far one of the most common and effective methods to investigate such a process. This possibility in turn rests on the reliability of the probe/labels involved. Here we present evidences of the effe…

Protein StructureSecondaryAβ(1–40) peptideAmyloidProtein ConformationMolecular Sequence DataBiophysicsSupramolecular chemistryMolecular Dynamics SimulationProtein aggregationProtein Aggregation PathologicalBiochemistryProtein Structure SecondarySupramolecular assemblyProtein Aggregateschemistry.chemical_compoundProtein structureAlzheimer DiseasePathologicalSecondary structureAβ(1-40) peptideHumansBenzothiazolesAmino Acid SequenceFluorescent DyesAmyloid beta-PeptidesProtein StabilityOrganic ChemistryAlzheimer's diseaseProtein AggregationSmall moleculePeptide FragmentsSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)Peptide ConformationAlzheimer's disease; Aβ(1–40) peptide; Protein aggregation; Protein conformation; Secondary structure; Thioflavin T; Alzheimer Disease; Amino Acid Sequence; Amyloid beta-Peptides; Fluorescence Recovery After Photobleaching; Fluorescent Dyes; Humans; Molecular Dynamics Simulation; Molecular Sequence Data; Peptide Fragments; Protein Aggregates; Protein Aggregation Pathological; Protein Conformation; Protein Multimerization; Protein Stability; Protein Structure Secondary; ThiazolesThiazolesBiophysicBiochemistrychemistryThioflavin TBiophysicsThioflavinProtein MultimerizationFluorescence Recovery After PhotobleachingBiophysical Chemistry
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