2017
Integrating mass spectrometry with MD simulations reveals the role of lipids in Na+/H+ antiporters
Landreh M, Marklund EG, Uzdavinys P, Degiacomi MT, Coincon M, Gault J, Gupta K, Liko I, Benesch JL, Drew D, Robinson CV. Integrating mass spectrometry with MD simulations reveals the role of lipids in Na+/H+ antiporters. Nature Communications 2017, 8: 13993. PMID: 28071645, PMCID: PMC5234078, DOI: 10.1038/ncomms13993.Peer-Reviewed Original ResearchConceptsIon mobility mass spectrometryGas phaseMass spectrometryMobility mass spectrometryMolecular dynamics simulationsCatalysis rateMD simulationsLipid-binding propertiesDynamics simulationsConformational stabilityStable dimerLarge-scale conformational changesSecondary active transportersConformational changesSpectrometryAntiporter NhaAKingdoms of lifeAnnular lipidsNative foldProtein segmentsInter-domain contactsRole of lipidsThermus thermophilusMembrane lipidsNHA2
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 ResearchConceptsMethanocaldococcus 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