Search results for "Free-electron laser"

showing 8 items of 8 documents

2020

Time-resolved photoemission with ultrafast pump and probe pulses is an emerging technique with wide application potential. Real-time recording of nonequilibrium electronic processes, transient states in chemical reactions, or the interplay of electronic and structural dynamics offers fascinating opportunities for future research. Combining valence-band and core-level spectroscopy with photoelectron diffraction for electronic, chemical, and structural analyses requires few 10 fs soft X-ray pulses with some 10 meV spectral resolution, which are currently available at high repetition rate free-electron lasers. We have constructed and optimized a versatile setup commissioned at FLASH/PG2 that c…

010302 applied physicsMicroscopePhotonMaterials scienceResolution (electron density)Free-electron laserLaser01 natural sciences010305 fluids & plasmaslaw.inventionMomentumTime of flightlaw0103 physical sciencesAtomic physicsInstrumentationUltrashort pulseReview of Scientific Instruments
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Femtosecond structural dynamics drives the trans/cis isomerization in photoactive yellow protein

2016

Many biological processes depend on detecting and responding to light. The response is often mediated by a structural change in a protein that begins when absorption of a photon causes isomerization of a chromophore bound to the protein. Pande et al. used x-ray pulses emitted by a free electron laser source to conduct time-resolved serial femtosecond crystallography in the time range of 100 fs to 3 ms. This allowed for the real-time tracking of the trans-cis isomerization of the chromophore in photoactive yellow protein and the associated structural changes in the protein.Science, this issue p. 725A variety of organisms have evolved mechanisms to detect and respond to light, in which the re…

0301 basic medicinePhotoreceptorsTime FactorsPhotoisomerizationLightProtein ConformationPhotochemistryPhotoreceptors MicrobialMYOGLOBINProtein structureMicrobialX-RAY-DIFFRACTIONPHOTOISOMERIZATIONMOTIONSchromophoresta116MultidisciplinarySPECTROSCOPYCrystallographyChemistryPhotochemical ProcessesTime resolved crystallographyTIMEMultidisciplinary SciencesPicosecondFemtosecondphotoactive proteinsScience & Technology - Other Topicsddc:500IsomerizationStereochemistryGeneral Science & TechnologyConjugated systemArticle03 medical and health sciencesBacterial ProteinsIsomerismEXCITATIONx-ray crystallographyPhotonsScience & TechnologyPHOTOCYCLEta114CHROMOPHOREta1182PATHWAYSChromophore030104 developmental biologyfree-electron laserssense organstrans-cis isomerization
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Two-Color Radiation Generated in a Seeded Free-Electron Laser with Two Electron Beams.

2015

We present the experimental evidence of the generation of coherent and statistically stable two-color free-electron laser radiation obtained by seeding an electron beam double peaked in energy with a laser pulse single spiked in frequency. The radiation presents two neat spectral lines, with time delay, frequency separation, and relative intensity that can be accurately controlled. The analysis of the emitted radiation shows a temporal coherence and a shot-to-shot regularity in frequency significantly enhanced with respect to the self-amplified spontaneous emission. © 2015 American Physical Society. © 2015 American Physical Society.

General Physics and AstronomyColorElectronsElectronseeding FELRadiation01 natural scienceslaw.inventionPhysics and Astronomy (all)OpticsColor Computer Simulation Image Processing Computer-Assisted Spectrum Analysis Electrons LaserslawFrequency separation0103 physical sciencesElectron beams; free electron lasers; physicsImage Processing Computer-AssistedSpontaneous emissionComputer Simulation010306 general physicsPhysicsFEL010308 nuclear & particles physicsbusiness.industryLasersSpectrum AnalysisSettore FIS/01 - Fisica SperimentaleFree-electron laserElectron beamsSPARCLaserFEL seeding FEL lasersFree Electron Laserfree electron lasersCathode raybusinessSeeded FELphysicsCoherence (physics)Physical review letters
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Ultrafast Dynamics of Magnetic Domain Structures Probed by Coherent Free-Electron Laser Light

2013

Synchrotron radiation news 26(6), 27 - 32 (2013). doi:10.1080/08940886.2013.850384

Nuclear and High Energy PhysicsMagnetic domainMagnetismAstrophysics::High Energy Astrophysical Phenomena02 engineering and technology53001 natural scienceslaw.inventionOpticslaw0103 physical sciencesddc:530010306 general physicsComputingMilieux_MISCELLANEOUSPhysicsMagnetic circular dichroismbusiness.industryScatteringFree-electron laser021001 nanoscience & nanotechnologyLaserAtomic and Molecular Physics and Optics[PHYS.COND.CM-MS]Physics [physics]/Condensed Matter [cond-mat]/Materials Science [cond-mat.mtrl-sci]Physics::Accelerator PhysicsAtomic physics0210 nano-technologybusinessUltrashort pulseFermi Gamma-ray Space TelescopeSynchrotron Radiation News
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Probing ultrafast changes of spin and charge density profiles with resonant XUV magnetic reflectivity at the free-electron laser FERMI

2017

We report the results of resonant magnetic XUV reflectivity experiments performed at the XUV free-electron laser FERMI. Circularly polarized XUV light with the photon energy tuned to the Fe M2,3 edge is used to measure resonant magnetic reflectivities and the corresponding Q-resolved asymmetry of a Permalloy/Ta/Permalloy trilayer film. The asymmetry exhibits ultrafast changes on 240 fs time scales upon pumping with ultrashort IR laser pulses. Depending on the value of the wavevector transfer Qz, we observe both decreasing and increasing values of the asymmetry parameter, which is attributed to ultrafast changes in the vertical spin and charge density profiles of the trilayer film.

Permalloy530 Physicsmedia_common.quotation_subjectPhysics::Optics02 engineering and technologyPhoton energy01 natural sciencesAsymmetrylaw.inventionARTICLESCondensed Matter::Materials Sciencelaw0103 physical scienceslcsh:QD901-999010306 general physicsSpin (physics)InstrumentationSpectroscopymedia_commonPhysicsRadiationCondensed matter physicsFree-electron laserCharge densitySurfaces and Interfaces530 Physik021001 nanoscience & nanotechnologyCondensed Matter PhysicsLaserlcsh:CrystallographyAtomic physics0210 nano-technologyUltrashort pulseStructural Dynamics
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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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Visualizing a protein quake with time-resolved X-ray scattering at a free-electron laser

2014

We describe a method to measure ultrafast protein structural changes using time-resolved wide-angle X-ray scattering at an X-ray free-electron laser. We demonstrated this approach using multiphoton excitation of the Blastochloris viridis photosynthetic reaction center, observing an ultrafast global conformational change that arises within picoseconds and precedes the propagation of heat through the protein. This provides direct structural evidence for a 'protein quake': the hypothesis that proteins rapidly dissipate energy through quake-like structural motions. peerReviewed

Photosynthetic reaction centreMaterials scienceProtein ConformationPhysics::OpticsPhycobiliproteinsfrequency vibrational-modesRadiation DosageBiochemistryMolecular physicsArticlelaw.inventionProtein structureX-Ray Diffractionlawddc:570Scattering Small AngleMolecular Biologyta116Quantitative Biology::BiomoleculesScatteringLasersMolecular biophysicsFree-electron laserCell BiologyLaserstructural dynamicsEnergy TransferPicosecondBiophysicsUltrashort pulseBiotechnologyNature methods
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2015

AbstractLight absorption can trigger biologically relevant protein conformational changes. The light-induced structural rearrangement at the level of a photoexcited chromophore is known to occur in the femtosecond timescale and is expected to propagate through the protein as a quake-like intramolecular motion. Here we report direct experimental evidence of such ‘proteinquake’ observed in myoglobin through femtosecond X-ray solution scattering measurements performed at the Linac Coherent Light Source X-ray free-electron laser. An ultrafast increase of myoglobin radius of gyration occurs within 1 picosecond and is followed by a delayed protein expansion. As the system approaches equilibrium i…

Quantitative Biology::Biomolecules0303 health sciencesMultidisciplinaryMaterials sciencePhotodissociationFree-electron laserGeneral Physics and Astronomy02 engineering and technologyGeneral ChemistryChromophore021001 nanoscience & nanotechnologyMolecular physicsGeneral Biochemistry Genetics and Molecular Biology03 medical and health scienceschemistry.chemical_compoundMyoglobinchemistryPicosecondFemtosecondRadius of gyrationsense organsPhysics::Chemical Physics0210 nano-technologyUltrashort pulse030304 developmental biologyNature Communications
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