2011
Mass spectrometric identification of an intramolecular disulfide bond in thermally inactivated triosephosphate isomerase from a thermophilic organism Methanocaldococcus jannaschii
Banerjee M, Gupta K, Balaram H, Balaram P. Mass spectrometric identification of an intramolecular disulfide bond in thermally inactivated triosephosphate isomerase from a thermophilic organism Methanocaldococcus jannaschii. Rapid Communications In Mass Spectrometry 2011, 25: 1915-1923. PMID: 21698673, DOI: 10.1002/rcm.5058.Peer-Reviewed Original ResearchMeSH KeywordsBacterial ProteinsCircular DichroismDisulfidesHot TemperatureMethanococcalesPeptide FragmentsProtein UnfoldingSequence Analysis, ProteinSpectrometry, Mass, Electrospray IonizationTandem Mass SpectrometryTriose-Phosphate IsomeraseConceptsMethanocaldococcus jannaschiiTriosephosphate isomeraseDisulfide bond formationIntramolecular disulfide bondsCysteine thiol groupsMonomer molecular massThree-dimensional structureThermophilic enzymesMass spectrometric identificationMS/MS analysisTetrameric enzymeTertiary structureMolecular massDisulfide bridgesDisulfide-bonded moleculesDisulfide bondsMonomeric massJannaschiiCircular dichroismComplete lossSpectrometric identificationIsomeraseEnzymeTryptic digestDa difference
2009
Identification of α- and β-hydroxy acid containing cyclodepsipeptides in natural peptide mixtures using negative ion mass spectrometry
Thakur SS, Ranganayaki RS, Gupta K, Balaram P. Identification of α- and β-hydroxy acid containing cyclodepsipeptides in natural peptide mixtures using negative ion mass spectrometry. Journal Of The American Society For Mass Spectrometry 2009, 20: 2221-2228. PMID: 19811932, DOI: 10.1016/j.jasms.2009.08.010.Peer-Reviewed Original ResearchAlgorithmsAnionsComplex MixturesDepsipeptidesFungal ProteinsHydroxy AcidsSpectrometry, Mass, Electrospray Ionization