ArticleJournal of the American Society for Mass Spectrometry2011
Gas-phase fragmentation of [M+nH+OH]n•+ ions formed from peptides containing intra-molecular disulfide bonds.
Article in Journal of the American Society for Mass Spectrometry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Assigning Peptide Disulfide Linkage Pattern Among Regio-Isomers via Methoxy Addition to Disulfide and Tandem Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2017Article
- Neo-Epitopes Generated on Hydroxyl Radical Modified GlycatedIgG Have Role in Immunopathology of Diabetes Type 2.PloS one · 2017Article
- Selective Gas-Phase Ion/Ion Reactions: Enabling Disulfide Mapping via Oxidation and Cleavage of Disulfide Bonds in Intermolecularly-Linked Polypeptide Ions.Analytical chemistry · 2016Article
- Reactions of hydroxyalkyl radicals with cysteinyl peptides in a nanoESI plume.Journal of the American Society for Mass Spectrometry · 2014Article
- Characterization of a DAPI-RIT-DAPI system for gas-phase ion/molecule and ion/ion reactions.Journal of the American Society for Mass Spectrometry · 2014Article
- Gas-phase reactivity of peptide thiyl (RS•), perthiyl (RSS•), and sulfinyl (RSO•) radical ions formed from atmospheric pressure ion/radical reactions.Journal of the American Society for Mass Spectrometry · 2013Article
- Gas-phase peptide sulfinyl radical ions: formation and unimolecular dissociation.Journal of the American Society for Mass Spectrometry · 2012Article
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In this study, we systematically investigated gas-phase fragmentation behavior of [M + nH + OH](n•+) ions formed from peptides containing intra-molecular disulfide bond. Backbone fragmentation and radical initiated neutral losses were observed as the two competing processes upon low energy collision-induced dissociation (CID). Their relative contribution was found to be affected by the charge state (n) of [M + nH + OH](n•+) ions and the means for activation, i.e., beam-type CID or ion trap CID. Radical initiated neutral losses were promoted in ion-trap CID and for lower charge states where mobile protons were limited. Beam-type CID and dissociation of higher charge states of [M + nH + OH](n•+) ions generally gave abundant backbone fragmentation, which was highly desirable for characterizing peptides containing disulfide bonds. The amount of sequence information obtained from CID of [M + nH + OH](n•+) ions was compared with that from CID of disulfide bond reduced peptides. For the 11 peptides studied herein, similar extent of sequence information was obtained from these two methods.
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