Observation of phosphorylation site-specific dissociation of singly protonated phosphopeptides

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Title
Observation of phosphorylation site-specific dissociation of singly protonated phosphopeptides
Author(s)
Y S Shin; Jeong Hee Moon; M S Kim
Bibliographic Citation
Journal of American Society for Mass Spectrometry, vol. 21, no. 1, pp. 53-59
Publication Year
2010
Abstract
In ultraviolet photodissociation of phosphopeptide ions with a basic residue (arginine, lysine, or histidine) at the N-terminus, intense an - 97 peaks were observed. These ions were formed by cleavage at phosphorylated residues only. For multiply phosphorylated peptides, this site-specific cleavage occurred at every phosphorylated residue. H/D exchange studies showed that an - 97 was formed by H3PO4 loss from an + 1 radical cations. The site-specificity of phosphate loss observed here is in contrast to the nonspecific phosphate loss from bn and yn reported previously. Characteristics of the reaction and its potential utility for phosphopeptide analysis are discussed.
ISSN
1044-0305
Publisher
Amer Soc Mass Spectr
DOI
http://dx.doi.org/10.1016/j.jasms.2009.09.003
Type
Article
Appears in Collections:
Division of Bio Technology Innovation > Core Research Facility & Analysis Center > 1. Journal Articles
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