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dc.contributor.authorKaszycki, Julia L.
dc.contributor.authorBowman, Andrew P.
dc.contributor.authorShvartsburg, Alexandre A.
dc.date.accessioned2016-06-13T13:49:19Z
dc.date.available2016-06-13T13:49:19Z
dc.date.issued2016-05
dc.identifier.citationKaszycki, Julia L.; Bowman, Andrew P.; Shvartsburg, Alexandre A. 2016. Ion mobility separation of peptide isotopomers. Journal of The American Society for Mass Spectrometry, vol. 27:no. 5:pp 795-799en_US
dc.identifier.issn1044-0305
dc.identifier.otherWOS:000374577600004
dc.identifier.urihttp://dx.doi.org/10.1007/s13361-016-1367-3
dc.identifier.urihttp://hdl.handle.net/10057/12074
dc.descriptionClick on the DOI link to access the article (may not be free).en_US
dc.description.abstractDifferential or field asymmetric waveform ion mobility spectrometry (FAIMS) operating at high electric fields fully resolves isotopic isomers for a peptide with labeled residues. The naturally present isotopes, alone and together with targeted labels, also cause spectral shifts that approximately add for multiple heavy atoms. Separation qualitatively depends on the gas composition. These findings may enable novel strategies in proteomic and metabolomic analyses using stable isotope labeling.en_US
dc.description.sponsorshipNIH K-INBRE (P20 GM103418) and NSF EPSCoR (EPS-0903806).en_US
dc.language.isoen_USen_US
dc.publisherSpringer International Publishing AGen_US
dc.relation.ispartofseriesJournal of The American Society for Mass Spectrometry;v.27:no.5
dc.subjectIon mobility spectrometryen_US
dc.subjectDifferential IMS (FAIMS)en_US
dc.subjectIsotopic analysesen_US
dc.subjectIsotopomersen_US
dc.titleIon mobility separation of peptide isotopomersen_US
dc.typeArticleen_US
dc.rights.holder© Springer International Publishing AG, Part of Springer Science+Business Mediaen_US


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