2017
Parallel folding pathways of Fip35 WW domain explained by infrared spectra and their computer simulation
Zanetti‐Polzi L, Davis CM, Gruebele M, Dyer RB, Amadei A, Daidone I. Parallel folding pathways of Fip35 WW domain explained by infrared spectra and their computer simulation. FEBS Letters 2017, 591: 3265-3275. PMID: 28881468, PMCID: PMC5658256, DOI: 10.1002/1873-3468.12836.Peer-Reviewed Original ResearchAmino Acid MotifsKineticsModels, MolecularMolecular Dynamics SimulationNIMA-Interacting Peptidylprolyl IsomeraseProtein Conformation, alpha-HelicalProtein Conformation, beta-StrandProtein DomainsProtein EngineeringProtein FoldingProtein UnfoldingQuantum TheorySpectrophotometry, InfraredThermodynamicsDual 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 ResearchMeSH KeywordsDeuterium OxideKineticsProteinsSpectrometry, FluorescenceSpectrophotometry, InfraredTemperatureTime FactorsConceptsQuantum 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
2015
Fast Helix Formation in the B Domain of Protein A Revealed by Site-Specific Infrared Probes
Davis CM, Cooper AK, Dyer RB. Fast Helix Formation in the B Domain of Protein A Revealed by Site-Specific Infrared Probes. Biochemistry 2015, 54: 1758-1766. PMID: 25706439, PMCID: PMC4356530, DOI: 10.1021/acs.biochem.5b00037.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceCircular DichroismInfrared RaysKineticsMethionineMolecular Dynamics SimulationMolecular ProbesMolecular Sequence DataPeptidesProtein FoldingProtein Structure, SecondaryProtein Structure, TertiarySpectrophotometry, InfraredSpectroscopy, Fourier Transform InfraredStaphylococcal Protein AConceptsLaser-induced temperatureWavelength-dependent measurementsSite-specific infrared probeMicrosecond phaseSubmillisecond time scaleIntermediate stateRelaxation kineticsComputational proteinInfrared probeStructural resolutionTime scalesSingle residue levelSpectroscopyTransition statePeptide backboneExperimental evidenceProbeResolutionMeasurementsComputer simulationsDirect measureHelical structureStatePartial formationAmide I region
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 ResearchMeSH KeywordsKineticsProtein FoldingProtein Structure, TertiarySpectrophotometry, InfraredSpectrophotometry, UltravioletConceptsLaser-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