2024
Beyond the “spine of hydration”: Chiral SFG spectroscopy detects DNA first hydration shell and base pair structures
Perets E, Konstantinovsky D, Santiago T, Videla P, Tremblay M, Velarde L, Batista V, Hammes-Schiffer S, Yan E. Beyond the “spine of hydration”: Chiral SFG spectroscopy detects DNA first hydration shell and base pair structures. The Journal Of Chemical Physics 2024, 161: 095104. PMID: 39230381, PMCID: PMC11377083, DOI: 10.1063/5.0220479.Peer-Reviewed Original ResearchConceptsChiral SFG spectraProbe water moleculeWater moleculesChiral SFG spectroscopyHydration shellSFG spectraMinor grooveSFG spectroscopyHydration shell water moleculesWater structureO-H stretching of waterSum frequency generation spectroscopyShell water moleculesPhosphate backboneN-H stretchingO-H stretchingDNA base pairsDNA minor grooveSpine of hydrationSpectra of DNAN-HVibrational spectroscopyO-HSFG responseSFG signalTheoretical basis for interpreting heterodyne chirality-selective sum frequency generation spectra of water
Konstantinovsky D, Santiago T, Tremblay M, Simpson G, Hammes-Schiffer S, Yan E. Theoretical basis for interpreting heterodyne chirality-selective sum frequency generation spectra of water. The Journal Of Chemical Physics 2024, 160: 055102. PMID: 38341693, PMCID: PMC10846909, DOI: 10.1063/5.0181718.Peer-Reviewed Original ResearchChiral SFG spectraSFG spectraVibrational bandsHydration shellO-H stretching modesVibrational sum frequency generationLorentzian functionO–H vibrational bandsSum frequency generation spectraIntramolecular vibrational couplingO–H stretching vibration bandsStretching vibration bandHydration waterSum frequency generationO-H stretchingHydration shells of biomoleculesVibrational frequency distributionDynamics of hydration waterGeneration spectraSpectral fittingInteraction of waterStretching modeVibrational couplingInduced chiralityO-H
2018
CO2 Reduction Catalysts on Gold Electrode Surfaces Influenced by Large Electric Fields
Clark M, Ge A, Videla P, Rudshteyn B, Miller C, Song J, Batista V, Lian T, Kubiak C. CO2 Reduction Catalysts on Gold Electrode Surfaces Influenced by Large Electric Fields. Journal Of The American Chemical Society 2018, 140: 17643-17655. PMID: 30468391, DOI: 10.1021/jacs.8b09852.Peer-Reviewed Original ResearchInterfacial electric fieldSum frequency generation spectroscopyStark tuning rateReduction catalystAu electrodePotential-dependent frequency shiftNew catalytic electrodesCO2 reduction catalystsGold electrode surfaceFrequency generation spectroscopySite of CODensity functional theoryMolecular catalystsCatalytic electrodesElectrode surfaceCarbonyl ligandsHeterogeneous catalystsTuning rateSemiconductor electrodesGeneration spectroscopyInterfacial fieldSFG spectraCatalystVibrational spectraExperimental frequency shifts
2016
Orientation of Cyano-Substituted Bipyridine Re(I) fac-Tricarbonyl Electrocatalysts Bound to Conducting Au Surfaces
Clark M, Rudshteyn B, Ge A, Chabolla S, Machan C, Psciuk B, Song J, Canzi G, Lian T, Batista V, Kubiak C. Orientation of Cyano-Substituted Bipyridine Re(I) fac-Tricarbonyl Electrocatalysts Bound to Conducting Au Surfaces. The Journal Of Physical Chemistry C 2016, 120: 1657-1665. DOI: 10.1021/acs.jpcc.5b10912.Peer-Reviewed Original ResearchSum frequency generation spectroscopyGold surfaceAu surfaceCO2 reduction catalystsFrequency generation spectroscopyReduction of CO2Density functional theoryMolecular catalystsReduction catalystBipyridine ligandsElectrochemical experimentsGeneration spectroscopyCatalytic turnoverSFG spectraElectrocatalystsFunctional theoryCatalystWeak bindingTheoretical methodsSurfaceBipyridineCatalysisSpectroscopyLigandsTriply
2013
Membrane Permeation Induced by Aggregates of Human Islet Amyloid Polypeptides
Poojari C, Xiao D, Batista V, Strodel B. Membrane Permeation Induced by Aggregates of Human Islet Amyloid Polypeptides. Biophysical Journal 2013, 105: 2323-2332. PMID: 24268144, PMCID: PMC3838749, DOI: 10.1016/j.bpj.2013.09.045.Peer-Reviewed Original ResearchConceptsChiral sum frequency generation (SFG) spectroscopySum frequency generation spectroscopyMembrane/water interfaceFrequency generation spectroscopyΒ-sheet secondary structureChannel-forming proteinMolecular dynamics simulationsSimulated SFG spectraAmphiphilic propertiesHuman islet amyloidGeneration spectroscopySFG spectraWater interfaceΒ-sandwichHuman islet amyloid polypeptideIslet β-cellsAmyloid polypeptideWater permeationDynamics simulationsHIAPP aggregatesSecondary structureMembrane permeationIslet amyloid polypeptideΒ-cellsFibrillar structures
2011
Chiral Sum Frequency Generation Spectroscopy for Characterizing Protein Secondary Structures at Interfaces
Fu L, Liu J, Yan EC. Chiral Sum Frequency Generation Spectroscopy for Characterizing Protein Secondary Structures at Interfaces. Journal Of The American Chemical Society 2011, 133: 8094-8097. PMID: 21534603, DOI: 10.1021/ja201575e.Peer-Reviewed Original ResearchConceptsChiral sum frequency generation (SFG) spectroscopySum frequency generation spectroscopyFrequency generation spectroscopyProtein secondary structureVibrational signaturesGeneration spectroscopyChiral SFG spectroscopyChiral SFG spectraRandom coilSecondary structureΑ-helixΒ-sheetLipid-water interfaceSFG spectroscopyHuman islet amyloidPeptide backboneSFG spectraH stretchAmide IReal-time characterizationSpectroscopyProtein conformationIslet amyloidStructureSitu
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