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dc.contributor.authorClark, Daniel Forrest
dc.contributor.authorGo, Eden P.
dc.contributor.authorToumi, Melinda L.
dc.contributor.authorDesaire, Heather
dc.identifier.citationClark, D. F., Go, E. P., Toumi, M. L., & Desaire, H. (2011). Collision Induced Dissociation Products of Disulfide-bonded Peptides: Ions Result from the Cleavage of More than One Bond. Journal of the American Society for Mass Spectrometry, 22(3), 492–498.
dc.descriptionThis document is the Accepted Manuscript version of a Published Work that appeared in final form in the Journal of the American Chemical Society, copyright © American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see
dc.description.abstractDisulfide bonds are a posttranslational modification (PTM) that can be scrambled or shuffled to non-native bonds during recombinant expression, sample handling, or sample purification. Currently, mapping of disulfide bonds is difficult due, to various sample requirements and data analysis difficulties. One step towards facilitating this difficult work is developing a better understanding of how disulfide-bonded peptides fragment during Collision Induced Dissociation (CID). Most automated analysis algorithms function based on the assumption that the preponderance of product ions observed during the dissociation of disulfide-bonded peptides result from the cleavage of just one peptide bond, and in this report we tested that assumption by extensively analyzing the product ions generated when several disulfide-bonded peptides are subjected to CID on a QTOF instrument. We found that one of the most common types of product ions generated resulted from two peptide bond cleavages, or a double cleavage. We found that for several of the disulfide-bonded peptides analyzed, the number of double cleavage product ions outnumbered those of single cleavages. The influence of charge state and precursor ion size was investigated, to determine if those parameters dictated the amount of double cleavage product ions formed. It was found in this sample set that no strong correlation existed between the charge state or peptide size and the portion of product ions assigned as double cleavages. This data shows that these ions could account for many of the product ions detected in CID data of disulfide bonded peptides. We also showed the utility of double cleavage product ions on a peptide with multiple cysteines present. Double cleavage products were able to fully characterize the bonding pattern of each cysteine where typical single b/y cleavage products could not.en_US
dc.publisherAmerican Chemical Societyen_US
dc.titleCollision Induced Dissociation Products of Disulfide-bonded Peptides: Ions Result from the Cleavage of More than One Bonden_US
kusw.kuauthorClark, Daniel F.
kusw.kuauthorGo, Eden P.
kusw.kuauthorToumi, Melinda L.
kusw.kuauthorDesaire, Heather
kusw.kudepartmentMedicinal Chemistryen_US
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kusw.oaversionScholarly/refereed, author accepted manuscripten_US
kusw.oapolicyThis item meets KU Open Access policy criteria.en_US

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