Apparent inhibition by arginine of macrocyclic b ion formation from singly charged protonated peptides

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Authors
Molesworth, Samuel P.
Van Stipdonk, Michael J.
Advisors
Issue Date
2010-08-01
Type
Article
Keywords
Research Support, Non-U.S. Gov't , Research Support, U.S. Gov't, Non-P.H.S.
Research Projects
Organizational Units
Journal Issue
Citation
Journal of the American Society for Mass Spectrometry. 2010 Aug; 21(8): 1322-8.
Abstract

There is now strong evidence for the existence of macrocyclic isomers of b(n)(+) ions, the formation and subsequent opening of which can lead to loss of sequence information from protonated peptides in multiple-stage tandem mass spectrometry experiments. In this study, the fragmentation patterns of protonated YARFLG and permuted isomers of the model peptide were investigated by collision-induced dissociation. Of interest was the potential influence of the arginine residue, and its position in the peptide sequence, on formation of the presumed macrocyclic b(5) ion isomer and potential loss of sequence information. We find that regardless of the sequence position (either internal or at the N- or C-terminus), only direct sequence ions or ions directly related to fragmentation of the arginine side chain are observed.

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Publisher
Springer
Journal
Book Title
Series
Journal of the American Society for Mass Spectrometry
J. Am. Soc. Mass Spectrom.
PubMed ID
DOI
ISSN
1879-1123
1044-0305
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