2012
Lipopeptides from the Banyan Endophyte, Bacillus subtilis K1: Mass Spectrometric Characterization of a Library of Fengycins
Pathak KV, Keharia H, Gupta K, Thakur SS, Balaram P. Lipopeptides from the Banyan Endophyte, Bacillus subtilis K1: Mass Spectrometric Characterization of a Library of Fengycins. Journal Of The American Society For Mass Spectrometry 2012, 23: 1716-1728. PMID: 22847390, DOI: 10.1007/s13361-012-0437-4.Peer-Reviewed Original ResearchConceptsHigh-performance liquid chromatographyMass spectrometryIonization mass spectrometric studyHigh-resolution mass spectrometryDiagnostic fragment ionsResolution mass spectrometryMass spectrometric characterizationMass spectrometric studyChain length variationReversed-phase high-performance liquid chromatographyMS/MS analysisLaser desorption ionizationMass spectrometric analysisLinear precursorsFragment ionsMacrocyclic ringFatty acid chainsPerformance liquid chromatographySpectrometric characterizationGlu replacementSpectrometric studyAcid moietyComplex mixturesDesorption ionizationFatty acid moieties
2010
Disulfide Bond Assignments by Mass Spectrometry of Native Natural Peptides: Cysteine Pairing in Disulfide Bonded Conotoxins
Gupta K, Kumar M, Balaram P. Disulfide Bond Assignments by Mass Spectrometry of Native Natural Peptides: Cysteine Pairing in Disulfide Bonded Conotoxins. Analytical Chemistry 2010, 82: 8313-8319. PMID: 20843009, DOI: 10.1021/ac101867e.Peer-Reviewed Original ResearchConceptsS bond cleavageBond cleavageNatural peptidesDisulfide bondsProduct ion yieldsMass spectral fragmentationDisulfide bond assignmentsDisulfide pairingFragment ionsStructure elucidationPeptide backboneBond assignmentDissociation conditionsMass spectrometryMultiple disulfide bondsCysteine pairingsSpectral fragmentationPossible disulfideMultiple cysteine residuesNative peptideAnalytical methodologyBondsCorrect disulfide pairingIon yieldFurther fragmentation