2024
Rapid Quantification of Protein Secondary Structure Composition from a Single Unassigned 1D 13C Nuclear Magnetic Resonance Spectrum
Li H, Tuttle M, Zilm K, Batista V. Rapid Quantification of Protein Secondary Structure Composition from a Single Unassigned 1D 13C Nuclear Magnetic Resonance Spectrum. Journal Of The American Chemical Society 2024, 146: 27542-27554. PMID: 39322561, DOI: 10.1021/jacs.4c08300.Peer-Reviewed Original ResearchMeSH KeywordsCarbon-13 Magnetic Resonance SpectroscopyNuclear Magnetic Resonance, BiomolecularProtein Structure, SecondaryProteinsConceptsSecondary structure compositionSecondary structureProtein secondary structure compositionEnsemble of secondary structuresSecondary structure elementsThree-dimensional foldC-NMR spectraSecondary structure contentProtein secondary structurePrimary sequenceProtein structureA-helixLiquid-liquid phase separationCharacterization of protein secondary structureMembrane-boundChemical shift assignmentsProteinBenchtop NMR spectrometersNuclear magnetic resonance spectraSolid-state NMRStructure contentRandom coilMagnetic resonance spectraB sheetsStructural composition
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 structuresChiral Sum Frequency Generation for In Situ Probing Proton Exchange in Antiparallel β‑Sheets at Interfaces
Fu L, Xiao D, Wang Z, Batista VS, Yan EC. Chiral Sum Frequency Generation for In Situ Probing Proton Exchange in Antiparallel β‑Sheets at Interfaces. Journal Of The American Chemical Society 2013, 135: 3592-3598. PMID: 23394622, PMCID: PMC9208335, DOI: 10.1021/ja3119527.Peer-Reviewed Original ResearchMeSH KeywordsDeuterium Exchange MeasurementPeptidesProtein Structure, SecondaryProtonsQuantum TheorySpectrum AnalysisConceptsD exchangeChiral sum frequency generation (SFG) spectroscopySum frequency generation spectroscopyHydrogen/deuterium exchangeSurface-selective methodFrequency generation spectroscopyVibrational modesAir/water interfaceAb initio simulationsWater OD stretch bandsH bondsPeptide backboneGeneration spectroscopyN stretchBulk solutionProton exchangeD stretchWater interfaceAntiparallel β-sheetDeuterium exchangeStretch bandFourier transformMass spectroscopyInitio simulations