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dc.contributor.authorPathak, Pratima
dc.contributor.authorBaird, Matthew A.
dc.contributor.authorShvartsburg, Alexandre A.
dc.date.accessioned2020-08-03T20:11:14Z
dc.date.available2020-08-03T20:11:14Z
dc.date.issued2020-06-05
dc.identifier.citationPratima Pathak, Matthew A. Baird, and Alexandre A. Shvartsburg. High-Resolution Ion Mobility Separations of Isomeric Glycoforms with Variations on the Peptide and Glycan Levels. Journal of the American Society for Mass Spectrometry 2020 31 (7), 1603-1609en_US
dc.identifier.issn1879-1123
dc.identifier.urihttps://doi.org/10.1021/jasms.0c00183
dc.identifier.urihttps://soar.wichita.edu/handle/10057/18876
dc.descriptionClick on the DOI link to access the article (may not be free).en_US
dc.description.abstractGlycosylation is a ubiquitous post-translational modification (PTM) that strongly affects the protein folding and function. Glycosylation patterns are impacted by many diseases, making promising biomarkers. Glycans are also the most complex PTMs, exhibiting isomers (linkage, anomers, and those with isomeric moieties). Permuted with localization variants that occur for all PTMs, these produce numerous isomeric glycoforms. Characterizing them by mass spectrometry and ion mobility spectrometry (IMS) has been a challenge. High-definition differential IMS (FAIMS) had robustly disentangled isomeric peptides involving other PTMs but was not evaluated for glycopeptides that featured multilevel isomerism. Here, we apply it to representative mucin glycopeptides with O-linked glycans: three GalNAc localization variants, a pair with α/β GalNAc anomers, and another with GalNAc/GlcNAc isomers. The first two classes were separated baseline with the resolution exceeding previous benchmarks by 10-fold, and the last pair was partly resolved. The recently demonstrated straightforward coupling to ultrahigh-resolution MS and electron-transfer dissociation makes high-definition FAIMS an attractive tool for glycoproteomics.en_US
dc.description.sponsorshipNSF CAREER Award (CHE-1552640) and NIH (1R01 GM134247). We thank Anastasia Sarycheva (WSU) for help with the data processing, and Daniel Delafield and Si Wu (U. of Oklahoma) for insightful discussions.en_US
dc.language.isoen_USen_US
dc.publisherAmerican Chemical Societyen_US
dc.relation.ispartofseriesJournal of the American Society for Mass Spectrometry;v.31:no.7
dc.subjectPeptides and proteinsen_US
dc.subjectCarbohydratesen_US
dc.subjectIonsen_US
dc.subjectMolecular structureen_US
dc.subjectChemical biologyen_US
dc.titleHigh-resolution ion mobility separations of isomeric glycoforms with variations on the peptide and glycan levelsen_US
dc.typeArticleen_US
dc.rights.holder© 2020, American Chemical Societyen_US


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