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dc.contributor.authorKaszycki, Julia L.
dc.contributor.authorShvartsburg, Alexandre A.
dc.identifier.citationKaszycki, J.L. & Shvartsburg, A.A. J. Am. Soc. Mass Spectrom. (2017) 28: 294en_US
dc.descriptionClick on the DOI link to access the article (may not be free).en_US
dc.description.abstractThe rising profile of ion mobility spectrometry (IMS) in proteomics has driven the efforts to predict peptide cross-sections. In the simplest approach, these are derived by adding the contributions of all amino acid residues and post-translational modifications (PTMs) defined by their intrinsic size parameters (ISPs). We show that the ISPs for PTMs can be calculated from properties of constituent atoms, and introduce the "impact scores" that govern the shift of cross-sections from the central mass-dependent trend for unmodified peptides. The ISPs and scores tabulated for 100 more common PTMs enable predicting the domains for modified peptides in the IMS/MS space that would guide subproteome investigations.en_US
dc.description.sponsorshipNIH K-INBRE (P20 GM103418), NSF First (EPS-0903806), and NSF CAREER (CHE-1552640).en_US
dc.publisherSpringer International Publishingen_US
dc.relation.ispartofseriesJournal of The American Society for Mass Spectrometry;v.28:no.2
dc.subjectIon mobility spectrometryen_US
dc.subjectPost-translational modificationsen_US
dc.titleA priori intrinsic PTM size parameters for predicting the ion mobilities of modified peptidesen_US
dc.rights.holder© 2017 Springer International Publishing AGen_US

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