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J Am Soc Mass Spectrom. 2007 Sep;18(9):1617-24. Epub 2007 Jun 19.

Sulfopeptide fragmentation in electron-capture and electron-transfer dissociation.

Author information

1
Mass Spectrometry Facility, Department of Pharmaceutical Chemistry, University of California San Francisco, San Francisco, California 94143-0446, USA. folkl@cgl.ucsf.edu

Abstract

Sulfopeptides can be misassigned as phosphopeptides because of the isobaric nature of the sulfo- and the phosphomoieties. Instruments having the ability to measure mass with high accuracy may be employed to distinguish these moieties based on their mass defect (the sulfo-group is 9 mmu lighter than the phosphomoiety). However, the assignment of the exact site(s) of post-translational modification is required to probe biological function. We have reported earlier that peptides with identical sequences containing either O-sulfo- or O-phospho-modifications display different fragmentation behavior (K. F. Medzihradszky et al., Mol. Cell. Proteom.2004, 3, 429-440). We have also established that O-sulfo moieties are susceptible to side-chain fragmentation during collision-induced dissociation. Our present study provides evidence that neutral SO(3) losses can also occur in electron capture dissociation and electron-transfer dissociation experiments. We also report that such neutral losses may be reduced by fragmenting peptide-alkali metal adducts, such as sodiated or potassiated peptides.

PMID:
17629708
DOI:
10.1016/j.jasms.2007.06.002
[Indexed for MEDLINE]
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