Search results for "Energy Transfer"

showing 10 items of 240 documents

Live cell imaging of duplex siRNA intracellular trafficking.

2015

Intracellular distribution of siRNA after in vitro transfection typically depends on lipopolyplexes, which must release the siRNA into the cytosol. Here, the fate of siRNAs was monitored by FRET-based live cell imaging. Subsequent to in situ observation of uptake and release processes, this approach allowed the observation of a number of hitherto uncharacterized intracellular distribution and degradation processes, commencing with a burst of endosomal releases, followed, in some cases, by fast siRNA influx into the nucleus. The continued observation of intact siRNA against a background of free fluorophores resulting from advanced degradation was possible by a specifically developed imaging …

Cell NucleusSmall interfering RNAMicroscopy ConfocalEndosomeTransfectionEndosomesBiologyTransfectionRNA TransportCell biologyCell LineRatsCytosolLive cell imagingCell cultureRNA interferenceGeneticsFluorescence Resonance Energy TransferAnimalsRNARNA Small InterferingIntracellularNucleic acids research
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Quantitative characterization of tetraspanin 8 homointeractions in the plasma membrane

2021

The spatial distribution of proteins in cell membranes is crucial for signal transduction, cell communication and membrane trafficking. Members of the Tetraspanin family organize functional protein clusters within the plasma membrane into so-called Tetraspanin-enriched microdomains (TEMs). Direct interactions between Tetraspanins are believed to be important for this organization. However, studies thus far have utilized mainly co-immunoprecipitation methods that cannot distinguish between direct and indirect, through common partners, interactions. Here we study Tetraspanin 8 homointeractions in living cells via quantitative fluorescence microscopy. We demonstrate that Tetraspanin 8 exists i…

Cell signalingTetraspaninsLipoylationDimerTransfectionBiochemistryArticleProtein–protein interactionchemistry.chemical_compoundMembrane MicrodomainsTetraspaninFluorescence Resonance Energy TransferHumansMolecular BiologyChemistryCell BiologyDissociation constantHEK293 CellsMembraneMicroscopy FluorescenceMembrane proteinembryonic structuresBiophysicsThermodynamicsProtein MultimerizationSignal transductionSignal TransductionBiochemical Journal
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Parallelized TCSPC for dynamic intravital fluorescence lifetime imaging : quantifying neuronal dysfunction in neuroinflammation

2013

Two-photon laser-scanning microscopy has revolutionized our view on vital processes by revealing motility and interaction patterns of various cell subsets in hardly accessible organs (e.g. brain) in living animals. However, current technology is still insufficient to elucidate the mechanisms of organ dysfunction as a prerequisite for developing new therapeutic strategies, since it renders only sparse information about the molecular basis of cellular response within tissues in health and disease. In the context of imaging, Forster resonant energy transfer (FRET) is one of the most adequate tools to probe molecular mechanisms of cell function. As a calibration-free technique, fluorescence lif…

Central Nervous SystemDiagnostic ImagingFluorescence-lifetime imaging microscopyPathologymedicine.medical_specialtyMouseScienceBiophysicsMedizinNeurophysiologyContext (language use)NeuroimagingBiosensing TechniquesBiologyIn Vitro TechniquesMiceCalcium imagingModel OrganismsMicroscopyMolecular Cell BiologyNeurobiology of Disease and RegenerationMedical imagingmedicineFluorescence Resonance Energy TransferAnimalsBiologyNeuroinflammationMultidisciplinaryPhysicsQRBrainAnimal ModelsIntravital ImagingCalcium ImagingFörster resonance energy transferMedicineCalciumFunction and Dysfunction of the Nervous SystemNeuroscienceResearch ArticleNeuroscience
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Comparison of quantum dot-binding protein tags: Affinity determination by ultracentrifugation and FRET

2013

Abstract Background Hybrid complexes of proteins and colloidal semiconductor nanocrystals (quantum dots, QDs) are of increasing interest in various fields of biochemistry and biomedicine, for instance for biolabeling or drug transport. The usefulness of protein–QD complexes for such applications is dependent on the binding specificity and strength of the components. Often the binding properties of these components are difficult and time consuming to assess. Methods In this work we characterized the interaction between recombinant light harvesting chlorophyll a / b complex (LHCII) and CdTe/CdSe/ZnS QDs by using ultracentrifugation and fluorescence resonance energy transfer (FRET) assay exper…

ChemistryBinding proteinBiophysicsNanoparticleProtein tagBiochemistryCrystallographyB vitaminsFörster resonance energy transferQuantum dotQuantum DotsFluorescence Resonance Energy TransferNanoparticlesUltracentrifugeChlorophyll Binding ProteinsUltracentrifugationMolecular BiologyBinding selectivityProtein BindingBiochimica et Biophysica Acta (BBA) - General Subjects
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Strong donor–acceptor couplings in a special pair-antenna model

2010

A special pair model composed of two cofacial zinc porphyrins (acceptor) linked to a free base (donor) acts as an energy transfer dyad. Despite the absence of conjugation, ππ*/charge transfer excited states and ultrafast energy transfer (∼5 ps) are noted.

ChemistryEnergy transferMetals and Alloyschemistry.chemical_elementFree baseCharge (physics)General ChemistryZincPhotochemistryMolecular physicsAcceptorCatalysisSurfaces Coatings and FilmsElectronic Optical and Magnetic MaterialsExcited stateMaterials ChemistryCeramics and CompositesAntenna (radio)Donor acceptorChemical Communications
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Three-dimensional orientational colocalization of individual donor--acceptor pairs.

2004

We report on the determination of the three-dimensional orientation of the donor and acceptor transition dipoles in individual fluorescence resonance energy transfer (FRET) pairs by means of scanning optical microscopy with annular illumination. Knowledge of the mutual orientation of the donor and acceptor dipole is mandatory for reliable distance determination based on FRET efficiency measurements. In our model system perylenediimide as the donor and terryelenediimide as the acceptor are coupled via a stiff p-terphenyl linker. The absorption dipoles of the donor and acceptor are selectively addressed by the 488 nm and 647 line of an Ar/Kr mixed gas laser, respectively. A clear deviation fr…

ChemistryGeneral Physics and AstronomyLaserFluorescenceAcceptorMolecular physicslaw.inventionDipoleCrystallographyFörster resonance energy transferOptical microscopelawPhysical and Theoretical ChemistryAbsorption (electromagnetic radiation)LinkerThe Journal of chemical physics
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Triplet exciplexes as energy transfer photosensitisers

2006

Experimental evidence is provided for the occurrence of triplet–triplet energy transfer from benzoylthiophene–indole exciplexes to naphthalenes with a remarkable stereodifferentiation; chiral recognition is also observed in the decay of the generated naphthalene triplets. Perez Prieto, Julia, Julia.Perez@uv.es ; Galian, Raquel Eugenia, Raquel.Galian@uv.es ; Morant Miñana, Maria Carmen, Maica.Morant@uv.es

Chiral recognitionStereochemistryEnergy transferUNESCO::QUÍMICAStereodifferentiationBenzoylthiophenePhotochemistry:QUÍMICA [UNESCO]CatalysisTriplet exciplexeschemistry.chemical_compoundMaterials ChemistryTriplet exciplexes ; Energy transfer ; Photosensitisers ; Benzoylthiophene ; Stereodifferentiation ; Chiral recognition ; NaphthalenePhysics::Chemical PhysicsNaphthaleneUNESCO::QUÍMICA::Química analíticaMetals and AlloysGeneral ChemistrySurfaces Coatings and FilmsElectronic Optical and Magnetic MaterialsPhotosensitiserschemistryEnergy transferCeramics and Composites:QUÍMICA::Química analítica [UNESCO]Naphthalene
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Towards the quantitative and physically-based interpretation of solar-induced vegetation fluorescence retrieved from global imaging

2021

Due to emerging high spectral resolution, remote sensing techniques and ongoing developments to retrieve the spectrally resolved vegetation fluorescence spectrum from several scales, the light reactions of photosynthesis are receiving a boost of attention for the monitoring of the Earth's carbon balance. Sensor-retrieved vegetation fluorescence (from leaf, tower, airborne or satellite scale) originating from the excited antenna chlorophyll a molecule has become a new quantitative biophysical vegetation parameter retrievable from space using global imaging techniques. However, to retrieve the actual quantum efficiencies, and hence a true photosynthetic status of the observed vegetation, all …

Chlorophyll aquantitative remote sensingPhysiologyEnergy transferBotanyPlant Sciencephotosynthesis monitoringReflectivityFluorescencechemistry.chemical_compoundchemistryQK1-989fluorescence quantum efficiencymedicineEnvironmental scienceflex-sentinel-3 tandem missionSatelliteSpectral resolutionmedicine.symptomScale (map)Vegetation (pathology)Remote sensingPhotosynthetica
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Consecutive binding of chlorophylls a and b during the assembly in vitro of light-harvesting chlorophyll-a/b protein (LHCIIb).

2006

The apoprotein of the major light-harvesting chlorophyll a/b complex (LHCIIb) is post-translationally imported into the chloroplast, where membrane insertion, protein folding, and pigment binding take place. The sequence and molecular mechanism of the latter steps is largely unknown. The complex spontaneously self-organises in vitro to form structurally authentic LHCIIb upon reconstituting the unfolded recombinant protein with the pigments chlorophyll a, b, and carotenoids in detergent micelles. Former measurements of LHCIIb assembly had revealed two apparent kinetic phases, a faster one (tau1) in the range of 10 s to 1 min, and a slower one (tau2) in the range of several min. To unravel th…

Chlorophyll bChlorophyllChlorophyll aTime FactorsPigment bindingLight-Harvesting Protein ComplexesModels BiologicalFluorescencechemistry.chemical_compoundStructural BiologyChlorophyll bindingAnimalsProtein Structure QuaternaryMolecular BiologyChlorophyll ACircular DichroismLight-harvesting complexes of green plantsChloroplastB vitaminsKineticsBiochemistrychemistryEnergy TransferChlorophyllBiophysicsChlamydomonas reinhardtiiProtein BindingJournal of molecular biology
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Random mutations directed to transmembrane and loop domains of the light-harvesting chlorophyll a/b protein: impact on pigment binding.

1999

The major light-harvesting complex of photosystem II (LHCII) can be reconstituted in vitro by folding its bacterially expressed apoprotein, Lhcb, in detergent solution in the presence of chlorophylls and carotenoids. To compare the impact of alpha-helical transmembrane domains and hydrophilic loop domains of the apoprotein on complex formation and stability, we introduced random mutations into a segment of the protein comprising the stromal loop, the third (C-proximal) transmembrane helix, and part of the amphipathic helix in the C-terminal domain. The mutant versions of Lhcb were screened for the loss of their ability to form stable LHCII upon reconstitution in vitro. Most steps during the…

Chlorophyll bChlorophyllProtein FoldingPigment bindingMolecular Sequence DataPhotosynthetic Reaction Center Complex ProteinsLight-Harvesting Protein ComplexesBiologyBiochemistryProtein Structure Secondarychemistry.chemical_compoundProtein structureChlorophyll bindingAmino Acid SequencePeptide sequencePeasMembrane ProteinsPhotosystem II Protein ComplexCarotenoidsTransmembrane proteinProtein Structure TertiaryTransmembrane domainSpectrometry FluorescencechemistryBiochemistryEnergy TransferMutationMutagenesis Site-DirectedProtein foldingProtein BindingBiochemistry
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