Characterization of complete histone tail proteoforms using differential ion mobility spectrometry

dc.contributor.authorShliaha, Pavel V.
dc.contributor.authorBaird, Matthew A.
dc.contributor.authorNielsen, Mogens M.
dc.contributor.authorGorshkov, Vladimir A.
dc.contributor.authorBowman, Andrew P.
dc.contributor.authorKaszycki, Julia L.
dc.contributor.authorJensen, Ole N.
dc.contributor.authorShvartsburg, Alexandre A.
dc.date.accessioned2017-06-11T18:13:23Z
dc.date.available2017-06-11T18:13:23Z
dc.date.issued2017-05-16
dc.descriptionACS AuthorChoice - This is an open access article published under an ACS AuthorChoice License, which permits copying and redistribution of the article or any adaptations for non-commercial purposes.en_US
dc.description.abstractHistone proteins are subject to dynamic post-translational modifications (PTMs) that cooperatively modulate the chromatin structure and function. Nearly all functional PTMs are found on the N-terminal histone domains (tails) of similar to 50 residues protruding from the nucleosome core. Using high-definition differential ion mobility spectrometry (FAIMS) with electron transfer dissociation, we demonstrate rapid baseline gas-phase separation and identification of tails involving rnonomethylation, trimethylation, acetylation, or phosphorylation in biologically relevant positions. These are by far the largest variant peptides resolved by any method, some with PTM contributing just 0.25% to the mass. This opens the door to similar separations for intact proteins and in top-down proteomics.en_US
dc.description.sponsorshipVILLUM Foundation to the VILLUM Center for Bioanalytical Sciences at University of Southern Denmark (O.N.J.), a Lundbeck Foundation Postdoctoral Fellowship (P.S.), and NIH COBRE (P30 GM110761) and NSF CAREER (CHE-1552640) grants (A.S.). A.S.en_US
dc.identifier.citationPavel V. Shliaha, Matthew A. Baird, Mogens M. Nielsen, Vladimir Gorshkov, Andrew P. Bowman, Julia L. Kaszycki, Ole N. Jensen, and Alexandre A. Characterization of complete histone tail proteoforms using differential ion mobility spectrometry. Analytical Chemistry 2017 89 (10), 5461-5466en_US
dc.identifier.issn0003-2700
dc.identifier.otherWOS:000401674800038
dc.identifier.urihttp://dx.doi.org/10.1021/acs.analchem.7b00379
dc.identifier.urihttp://hdl.handle.net/10057/13353
dc.language.isoen_USen_US
dc.publisherAmerican Chemical Societyen_US
dc.relation.ispartofseriesAnalytical Chemistry;v.89:no.10
dc.rights.holderCopyright © 2017 American Chemical Societyen_US
dc.subjectElectron-transfer dissociationen_US
dc.subjectEmbryonic stem-cellsen_US
dc.subjectMass-spectrometryen_US
dc.subjectPosttranslational modificationsen_US
dc.subjectFaims-msen_US
dc.subjectProteomicsen_US
dc.subjectProteinen_US
dc.subjectSeparationen_US
dc.subjectIonizationen_US
dc.subjectPhosphopeptidesen_US
dc.titleCharacterization of complete histone tail proteoforms using differential ion mobility spectrometryen_US
dc.typeArticleen_US
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