Apparent inhibition by arginine of macrocyclic b ion formation from singly charged protonated peptides
Molesworth, Samuel P. Van Stipdonk, Michael J.
Molesworth, Samuel P.
Van Stipdonk, Michael J.
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2010-08-01
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Article
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Research Support, Non-U.S. Gov't,Research Support, U.S. Gov't, Non-P.H.S.
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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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Springer
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Journal of the American Society for Mass Spectrometry
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1879-1123
1044-0305
1044-0305