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dc.contributor.authorGarabedian, Alyssa
dc.contributor.authorBaird, Matthew A.
dc.contributor.authorPorter, Jacob
dc.contributor.authorFouque, Kevin Jeanne Dit
dc.contributor.authorShliaha, Pavel V.
dc.contributor.authorJensen, Ole N.
dc.contributor.authorWilliams, Todd D.
dc.contributor.authorFernandez-Lima, Francisco
dc.contributor.authorShvartsburg, Alexandre A.
dc.date.accessioned2018-03-22T20:13:22Z
dc.date.available2018-03-22T20:13:22Z
dc.date.issued2018
dc.identifier.citationAlyssa Garabedian, Matthew A. Baird, Jacob Porter, Kevin Jeanne Dit Fouque, Pavel V. Shliaha, Ole N. Jensen, Todd D. Williams, Francisco Fernandez-Lima, and Alexandre A. Shvartsburg. Linear and Differential Ion Mobility Separations of Middle-Down Proteoforms. Analytical Chemistry, 2018 90 (4), 2918-2925en_US
dc.identifier.issn0003-2700
dc.identifier.otherWOS:000426143100072
dc.identifier.urihttp://dx.doi.org/10.1021/acs.analchem.7b05224
dc.identifier.urihttp://hdl.handle.net/10057/14700
dc.descriptionClick on the DOI link to access the article (may not be free).en_US
dc.description.abstractComprehensive characterization of proteomes comprising the same proteins with distinct post-translational modifications (PTMs) is a staggering challenge. Many such proteoforms are isomers (localization variants) that require separation followed by top-down or middle-down mass spectrometric analyses, but condensed-phase separations are ineffective in those size ranges. The variants for "middle-down" peptides were resolved by differential ion mobility spectrometry (FAIMS), relying on the mobility increment at high electric fields, but not previously by linear IMS on the basis of absolute mobility. We now use complete histone tails with diverse PTMs on alternative sites to demonstrate that high resolution linear IMS, here trapped IMS (TIMS), broadly resolves the variants of 50 residues in full or into binary mixtures quantifiable by tandem MS, largely thanks to orthogonal separations across charge states. Separations using traveling-wave (TWIMS) and/or involving various time scales and electrospray ionization source conditions are similar (with lower resolution for TWIMS), showing the transferability of results across linear IMS instruments. The linear IMS and FAIMS dimensions are substantially orthogonal, suggesting FAIMS/IMS/MS as a powerful platform for proteoform analyses.en_US
dc.description.sponsorshipNIH COBRE (P30 GM110761), NSF CAREER (CHE-1552640), NSF CAREER (CHE-1654274), NIH R21DA041287, and VILLUM and Lundbeck Foundations. Purchase of the Synapt G2 instrument was funded by NIH COBRE (P20 RR17708) and HRSA C76HF16266.en_US
dc.language.isoen_USen_US
dc.publisherAmerican Chemical Societyen_US
dc.relation.ispartofseriesAnalytical Chemistry;v.90:no.4
dc.subjectElectron-transfer dissociationen_US
dc.subjectTandem mass-spectrometryen_US
dc.subjectEmbryonic stem-cellsen_US
dc.subjectGas-phase separationsen_US
dc.subjectPosttranslational modificationsen_US
dc.subjectHistone tailsen_US
dc.subjectPeptideen_US
dc.subjectProteinen_US
dc.subjectResolutionen_US
dc.subjectMSen_US
dc.titleLinear and differential ion mobility separations of middle-down proteoformsen_US
dc.typeArticleen_US
dc.rights.holder© 2018, American Chemical Societyen_US


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