Search results for "Time-resolved spectroscopy"

showing 10 items of 39 documents

Time-resolved spectroscopy of ZnWO4

2001

The luminescence spectra of ZnWO 4 excited by a pulsed electron beam, pulsed nitrogen laser and X-ray are studied. The luminescence decay kinetics are compared with transient absorption relaxation kinetics. Broad band transient absorption spectra are observed and it is shown that the slow decay component (∼14 μs at RT) of the transient absorption matches well with the luminescence decay therefore this absorption is due to the excited state absorption of the luminescence center.

Nuclear and High Energy PhysicsRadiationAbsorption spectroscopyCondensed Matter::OtherChemistryRelaxation (NMR)Physics::OpticsCondensed Matter PhysicsExcited stateUltrafast laser spectroscopyGeneral Materials ScienceNitrogen laserAtomic physicsTime-resolved spectroscopyAbsorption (electromagnetic radiation)LuminescenceRadiation Effects and Defects in Solids
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Observing heme doming in myoglobin with femtosecond X-ray absorption spectroscopy.

2015

International audience; We report time-resolved X-ray absorption measurements after photolysis of carbonmonoxy myoglobin performed at the LCLS X-ray free electron laser with nearly 100 fs (FWHM) time resolution. Data at the Fe K-edge reveal that the photoinduced structural changes at the heme occur in two steps, with a faster (∼70 fs) relaxation preceding a slower (∼400 fs) one. We tentatively attribute the first relaxation to a structural rearrangement induced by photolysis involving essentially only the heme chromophore and the second relaxation to a residual Fe motion out of the heme plane that is coupled to the displacement of myoglobin F-helix

PhotodissociationAbsorption spectroscopyTime resolved spectroscopyInvited ArticlesPhotochemistrySPECIAL TOPIC: BIOLOGY WITH X-RAY LASERS 2chemistry.chemical_compoundX-ray absorption spectralcsh:QD901-999X-ray absorption near edge structureSpectroscopyInstrumentationHemeSpectroscopy[PHYS]Physics [physics]RadiationX-ray optics[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry Molecular Biology/Structural Biology [q-bio.BM]ChemistryPhotodissociationRelaxation (NMR)ChromophoreCondensed Matter PhysicsSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)MyoglobinBiofisica Dinamica delle proteine Spettroscopia risolta in tempo X-ray free-electron laser Assorbimento di raggi Xlcsh:CrystallographyTime-resolved spectroscopyStructural dynamics (Melville, N.Y.)
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Excitonic luminescence in ZnO nanopowders and ceramics

2009

Abstract Fast photoluminescence spectra in the spectral region of 3.1–3.45 eV in ZnO and ZnO:Al ceramics were studied at 14 and 300 K. Ceramics with grains smaller than 100 nm were sintered from nanopowders by high pressure (8 GPa) and low temperature (350 °C). Ceramics with grain sizes 1–5 μm were sintered at 1400 °C. It is shown that excitonic luminescence spectra depend on the ceramics grain size, post preparing annealing and doping. The excitonic luminescence decay time was faster than 2 ns and the afterglow at 30 ns was ∼0.05%.

PhotoluminescenceMaterials scienceAnnealing (metallurgy)Organic ChemistryDopingAnalytical chemistryMineralogyAtomic and Molecular Physics and OpticsGrain sizeElectronic Optical and Magnetic MaterialsAfterglowInorganic Chemistryvisual_artvisual_art.visual_art_mediumCeramicElectrical and Electronic EngineeringPhysical and Theoretical ChemistryTime-resolved spectroscopyLuminescenceSpectroscopyOptical Materials
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Exact reconstruction of thz sub-λ source features in knife-edge measurements

2013

The spatial features of a sub-wavelength terahertz source are not accessible using time-integrated knife-edge techniques due to the non-separable space-time nature of the radiated field and to systematic modifications induced by the blade itself. We show that combining knife-edge with a time resolved electro-optical sampling, the space-time coupling can be addressed and the source field profile can be exactly reconstructed.

PhysicsCouplingPhase-sensitive field characterizationBlade (geometry)Terahertz radiationbusiness.industrySettore ING-INF/02 - Campi ElettromagneticiEdge (geometry)Lambdasubwavelength sourceSettore ING-INF/01 - ElettronicaSource fieldAtomic and Molecular Physics and OpticsOpticsSampling (signal processing)subwavelength sourcesspatiotemporal field characterizationElectrical and Electronic EngineeringTime-resolved spectroscopybusinessterahertz (THz) sources
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Optical Spectroscopy of Short-Lived Isotopes

1979

This chapter will concentrate on a special branch of the large field of optical spectroscopy, namely, the study of hyperfine structure (hfs) and isotope shift (IS) of short-lived isotopes. Such investigations give information on some basic properties of these nuclei: the spin ( ), the magnetic moment (μI), the spectroscopic quadrupole moment (Q s ), and the change of the mean square charge radius between different isotopes (δ〈r 2〉).

PhysicsMagnetic momentCharge radiusQuadrupolePhysics::Atomic PhysicsSoft X-ray emission spectroscopyTime-resolved spectroscopyAtomic physicsNuclear ExperimentSpectroscopySpin (physics)Hyperfine structure
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Mechanism‐Dependent Modulation of Ultrafast Interfacial Water Dynamics in Intrinsically Disordered Protein Complexes

2018

Abstract The recognition of intrinsically disordered proteins (IDPs) is highly dependent on dynamics owing to the lack of structure. Here we studied the interplay between dynamics and molecular recognition in IDPs with a combination of time‐resolving tools on timescales ranging from femtoseconds to nanoseconds. We interrogated conformational dynamics and surface water dynamics and its attenuation upon partner binding using two IDPs, IBB and Nup153FG, both of central relevance to the nucleocytoplasmic transport machinery. These proteins bind the same nuclear transport receptor (Importinβ) with drastically different binding mechanisms, coupled folding–binding and fuzzy complex formation, resp…

Protein ConformationSolvation Dynamicsprotein–protein interactions010402 general chemistryIntrinsically disordered proteins01 natural sciencestime-resolved spectroscopyCatalysisProtein–protein interactionMolecular recognitionnucleocytoplasmic transport010405 organic chemistryMechanism (biology)ChemistryCommunicationWaterGeneral Chemistrybeta KaryopherinsCommunications0104 chemical sciencesIntrinsically Disordered ProteinsNucleocytoplasmic TransportModulationChemical physicsThermodynamicsTime-resolved spectroscopyNuclear transportAngewandte Chemie International Edition
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Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy

2014

Monitoring the dynamics of protonation and protein backbone conformation changes during the function of a protein is an essential step towards understanding its mechanism. Protonation and conformational changes affect the vibration pattern of amino acid side chains and of the peptide bond, respectively, both of which can be probed by infrared (IR) difference spectroscopy. For proteins whose function can be repetitively and reproducibly triggered by light, it is possible to obtain infrared difference spectra with (sub)microsecond resolution over a broad spectral range using the step-scan Fourier transform infrared technique. With -10(2)-10(3) repetitions of the photoreaction, the minimum num…

RhodopsinMaterials scienceproton transferProtein ConformationGeneral Chemical EngineeringBiophysicsAnalytical chemistryInfrared spectroscopymembrane proteinsProtonationtime-resolved spectroscopyGeneral Biochemistry Genetics and Molecular Biologychannelrhodopsinattenuated total reflectionProtein structureSpectroscopy Fourier Transform InfraredFourier transform infrared spectroscopyinfrared spectroscopySpectroscopyIssue 88biologyGeneral Immunology and MicrobiologybacteriorhodopsinGeneral Neurosciencesingular value decompositionstep-scanProteinsEspectroscòpia infrarojaBacteriorhodopsinPhotochemical ProcessesBacteriorhodopsinsAttenuated total reflectionprotein dynamicsbiology.proteinProtonsTime-resolved spectroscopyProteïnesJournal of Visualized Experiments
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Do fluorescence and transient absorption probe the same intramolecular charge transfer state of 4-(dimethylamino)benzonitrile?

2009

International audience; We present here the results of time-resolved absorption and emission experiments for 4-(dimethylamino)benzonitrile in solution, which suggest that the fluorescent intramolecular charge transfer (ICT) state may differ from the twisted ICT (TICT) state observed in transient absorption.

Time Factorstime resolved spectraGeneral Physics and Astronomyvisible spectra010402 general chemistryPhotochemistry01 natural sciencesTime resolved spectraSpectral lineFluorescencechemistry.chemical_compoundspectrochemical analysisOrganic compoundsUltrafast laser spectroscopyNitrilesCharge exchangePhysical and Theoretical ChemistryVisible spectra:FÍSICA::Química física [UNESCO]Fluorescent DyesSpectrochemical analysis010405 organic chemistryChemistrycharge exchangeFluorescenceUNESCO::FÍSICA::Química física0104 chemical sciences3. Good health[CHIM.THEO]Chemical Sciences/Theoretical and/or physical chemistryBenzonitrileIntramolecular forceCharge exchange ; Fluorescence ; Organic compounds ; Spectrochemical analysis ; Time resolved spectra ; Visible spectraAbsorption (chemistry)Time-resolved spectroscopyLuminescenceorganic compoundsThe Journal of chemical physics
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Cavités plasmoniques et nanosources optiques

2013

Optical microcavities exhibit high resonance quality, so that, they are of key interest for the design of low-threshold lasers or for achieving strong coupling regime. But, such systems support modes whose the volume remain diffraction limited.In this manuscript, we are interested in their plasmonic counterparts because they support confined modes at the sub-wavelength scale. First, we study an in-plane plasmonic cavity which is the transposition of 1D optical cavity to surface wave. We characterize the cavity by measuring the fluorescence lifetime of dye molecules deposited inside.Then, we are interested in 3-dimension mode confinement achieved by spherical metal nanoparticles. We discuss …

Time-resolved spectroscopyCavité plasmonique[SPI.OTHER]Engineering Sciences [physics]/Other[ SPI.OTHER ] Engineering Sciences [physics]/Other[SPI.OTHER] Engineering Sciences [physics]/OtherSpontaneous emissionSpectroscopie résolue en tempsLocalized surface plasmon[ PHYS.COND.CM-GEN ] Physics [physics]/Condensed Matter [cond-mat]/Other [cond-mat.other]Plasmonic cavity[PHYS.COND.CM-GEN] Physics [physics]/Condensed Matter [cond-mat]/Other [cond-mat.other][PHYS.COND.CM-GEN]Physics [physics]/Condensed Matter [cond-mat]/Other [cond-mat.other]Émission spontanéePlasmon de surface localisé
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Ultrafast excitation dynamics of low energy pigments in reconstituted peripheral light-harvesting complexes of photosystem I

2000

AbstractUltrafast dynamics of a reconstituted Lhca4 subunit from the peripheral LHCI-730 antenna of photosystem I of higher plants were probed by femtosecond absorption spectroscopy at 77 K. Intramonomeric energy transfer from chlorophyll (Chl) b to Chl a and energy equilibration between Chl a molecules observed on the subpicosecond time scale are largely similar to subpicosecond energy equilibration processes within LHCII monomers. However, a 5 ps equilibration process in Lhca4 involves unique low energy Chls in LHCI absorbing at 705 nm. These pigments localize the excitation both in the Lhca4 subunit and in LHCI-730 heterodimers. An additional 30–50 ps equilibration process involving red …

Time-resolved spectroscopyPhotosystem I0106 biological sciencesAbsorption spectroscopyPhotosynthetic Reaction Center Complex ProteinsLight-Harvesting Protein ComplexesBiophysicsPhotochemistryPhotosystem I01 natural sciences7. Clean energyBiochemistryFluorescence spectroscopyLight-harvesting complexExcitation energy transfer03 medical and health scienceschemistry.chemical_compoundStructural BiologyUltrafast laser spectroscopyGeneticsMolecular BiologyPlant Proteins030304 developmental biology0303 health sciencesPhotosystem I Protein ComplexSpectrophotometry AtomicPigments BiologicalCell BiologyPlantsLHCI-730 heterodimerEnergy TransferchemistryAntennaChlorophyllPicosecondChlorophyll Binding ProteinsLight-harvesting complexTime-resolved spectroscopyDimerization010606 plant biology & botanyFEBS Letters
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