2017
Dual time-resolved temperature-jump fluorescence and infrared spectroscopy for the study of fast protein dynamics
Davis CM, Reddish MJ, Dyer RB. Dual time-resolved temperature-jump fluorescence and infrared spectroscopy for the study of fast protein dynamics. Spectrochimica Acta Part A Molecular And Biomolecular Spectroscopy 2017, 178: 185-191. PMID: 28189834, PMCID: PMC5346054, DOI: 10.1016/j.saa.2017.01.069.Peer-Reviewed Original ResearchConceptsQuantum cascade lasersTime-resolved IRYAG laserTunable quantum cascade laserFluorescence spectroscopyProtein dynamicsAbsorbance detection limitCascade lasersSapphire laserComplex folding mechanismsLaserIR frequenciesOverall fluorescence intensityFluorescence spectrometerSpectroscopyIR spectrometerFluorescence measurementsFluorescence sensitivityHigh sensitivityT-jumpSpectrometerFast protein dynamicsFolding mechanismPowerful techniqueFluorescence
2014
WW Domain Folding Complexity Revealed by Infrared Spectroscopy
Davis CM, Dyer RB. WW Domain Folding Complexity Revealed by Infrared Spectroscopy. Biochemistry 2014, 53: 5476-5484. PMID: 25121968, PMCID: PMC4151701, DOI: 10.1021/bi500556h.Peer-Reviewed Original ResearchConceptsLaser-induced temperatureWavelength-dependent measurementsDry molten globule statesInfrared SpectroscopyProtein Folding DynamicsFBP28 WW domainCorresponding IR bandsRelaxation dynamicsSubmillisecond time scaleWild-type WW domainComplementary probesDry molten globuleSingle exponential kineticsAmide I regionFolding DynamicsFluorescence spectraFluorescence spectroscopyPeptide backboneMolten globule stateRelaxation kineticsConvenient probeSpectroscopyFluorescence measurementsIR bandsSide chains
1998
Synthesis and characterization of an internal emission standard and applications to fluorescence studies of photosystem II
Schweitzer R, Brudvig G. Synthesis and characterization of an internal emission standard and applications to fluorescence studies of photosystem II. Biopolymers 1998, 2: 167-171. DOI: 10.1002/(sici)1520-6343(1996)2:3<167::aid-bspy3>3.0.co;2-5.Peer-Reviewed Original ResearchChelate complexesFluorescence intensityFluorescence measurementsDiethylenetriaminepentaacetic acid derivativeTerbium luminescenceAqueous phaseTerbium emissionAcid derivativesPyrimidine ringComplexesPhotosystem II functionLow temperaturePhotosynthetic organismsLow absorptionCryogenic temperaturesLanthanidesDifferent samplesLigandsSynthesisLuminescenceTerbiumTemperatureDerivativesPurificationEmission standardsTime-Resolved Fluorescence Measurements of Photosystem II: The Effect of Quenching by Oxidized Chlorophyll Z
Schweitzer R, Melkozernov A, Blankenship R, Brudvig G. Time-Resolved Fluorescence Measurements of Photosystem II: The Effect of Quenching by Oxidized Chlorophyll Z. The Journal Of Physical Chemistry B 1998, 102: 8320-8326. DOI: 10.1021/jp982098y.Peer-Reviewed Original ResearchExciton equilibrationChlorophyll ZPhotosystem IIFluorescence measurementsSpinach PSII membranesCore antennaNanosecond decay componentTime-resolved fluorescence spectroscopyTime-resolved fluorescence measurementsPSII core complexesSteady-state fluorescence intensityPSII membranesChlZFluorescence spectroscopyLHCII antennaEffective quencherCore antenna chlorophyllsFluorescence decay timePotent quencher
1995
Optical signals from neurons with internally applied voltage-sensitive dyes
Antic S, Zecevic D. Optical signals from neurons with internally applied voltage-sensitive dyes. Journal Of Neuroscience 1995, 15: 1392-1405. PMID: 7869106, PMCID: PMC6577832, DOI: 10.1523/jneurosci.15-02-01392.1995.Peer-Reviewed Original ResearchConceptsOptical signalVoltage-sensitive dyeSilicon photodiode arrayAxonal branchesAction potentialsIndividual neuronsOptical monitoringPresent sensitivityPhotodiode arraySite of stimulationAction potential initiationLong axonal branchesSatisfactory signalIntracellular pressure injectionSynaptic potentialsFluorescence measurementsGood signalAxonal segmentsSubthreshold potentialsExtracellular applicationCell bodiesNeuronal processesFluorescence signalElectrotonic responsesPotential initiation
1988
Evaluation of 5-enolpyruvoylshikimate-3-phosphate synthase substrate and inhibitor binding by stopped-flow and equilibrium fluorescence measurements.
Anderson K, Sikorski J, Johnson K. Evaluation of 5-enolpyruvoylshikimate-3-phosphate synthase substrate and inhibitor binding by stopped-flow and equilibrium fluorescence measurements. Biochemistry 1988, 27: 1604-10. PMID: 3284585, DOI: 10.1021/bi00405a032.Peer-Reviewed Original ResearchConceptsBinding of substratesBinary complexShikimate 3-phosphateStopped-flow fluorescence methodsDissociation constantFree enzymeGlyphosate bindingS3P bindingInhibitor bindingProtein fluorescenceKinetics of bindingTernary complexEnzymeStopped-flowFluorescence measurementsBindingFluorescence titrationSaturating concentrationsS3PEquilibrium fluorescence measurements
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