2012
Distinct Disulfide Isomers of μ‑Conotoxins KIIIA and KIIIB Block Voltage-Gated Sodium Channels
Khoo KK, Gupta K, Green BR, Zhang MM, Watkins M, Olivera BM, Balaram P, Yoshikami D, Bulaj G, Norton RS. Distinct Disulfide Isomers of μ‑Conotoxins KIIIA and KIIIB Block Voltage-Gated Sodium Channels. Biochemistry 2012, 51: 9826-9835. PMID: 23167564, PMCID: PMC4131687, DOI: 10.1021/bi301256s.Peer-Reviewed Original ResearchConceptsΜ-Conotoxin KIIIADisulfide connectivityCollision-induced dissociation fragmentationDisulfide isomersNuclear magnetic resonance dataNative disulfide connectivityDisulfide patternVenom-derived peptidesDisulfide bond connectivitySame disulfide connectivityOxidative foldingDissociation fragmentationMagnetic resonance dataBond connectivityMultiple disulfide bondsMinor productsMajor isomerSolution structureActive peptidesIsomersΜ-conotoxinsResonance dataKIIIAVenom of ConusDisulfide bonds
2011
Combined Electron Transfer Dissociation–Collision-Induced Dissociation Fragmentation in the Mass Spectrometric Distinction of Leucine, Isoleucine, and Hydroxyproline Residues in Peptide Natural Products
Gupta K, Kumar M, Chandrashekara K, Krishnan KS, Balaram P. Combined Electron Transfer Dissociation–Collision-Induced Dissociation Fragmentation in the Mass Spectrometric Distinction of Leucine, Isoleucine, and Hydroxyproline Residues in Peptide Natural Products. Journal Of Proteome Research 2011, 11: 515-522. PMID: 22111579, DOI: 10.1021/pr200091v.Peer-Reviewed Original ResearchConceptsIsobaric residuesMass spectrometric peptide sequencingNatural peptide librariesPeptide natural productsCrude peptide mixturesTandem mass spectrometric methodMass spectrometric distinctionMass spectrometric methodRadical ionsIsobaric leucineElectron transferCollisional activationDissociation fragmentationPeptide mixturesNatural productsNominal massSpectrometric methodLiquid chromatographyPeptide sequencingPresence of hydroxyprolineIonsPeptide libraryDifferent peptidesDissociation approachHydroxyproline residues