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 ResearchConceptsSecondary 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
2022
Insights into Binding of Single-Stranded Viral RNA Template to the Replication–Transcription Complex of SARS-CoV‑2 for the Priming Reaction from Molecular Dynamics Simulations
Wang J, Shi Y, Reiss K, Allen B, Maschietto F, Lolis E, Konigsberg WH, Lisi GP, Batista VS. Insights into Binding of Single-Stranded Viral RNA Template to the Replication–Transcription Complex of SARS-CoV‑2 for the Priming Reaction from Molecular Dynamics Simulations. Biochemistry 2022, 61: 424-432. PMID: 35199520, PMCID: PMC8887646, DOI: 10.1021/acs.biochem.1c00755.Peer-Reviewed Original ResearchConceptsReplication-transcription complexPriming reactionRNA duplexesTemplate strandRNA templateHigher-order oligomerizationRNA-dependent RNA polymeraseCryo-EM structureRNA primaseViral RNA templateRNA polymerasePrimer synthesisViral transcriptionSecondary structureViral genomeSubunitsMolecular dynamics simulations
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