Observation of phosphorylation site-specific dissociation of singly protonated phosphopeptides

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dc.contributor.authorY S Shin-
dc.contributor.authorJeong Hee Moon-
dc.contributor.authorM S Kim-
dc.date.accessioned2017-04-19T09:17:14Z-
dc.date.available2017-04-19T09:17:14Z-
dc.date.issued2010-
dc.identifier.issn1044-0305-
dc.identifier.uri10.1016/j.jasms.2009.09.003ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/9352-
dc.description.abstractIn 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.-
dc.publisherAmer Soc Mass Spectr-
dc.titleObservation of phosphorylation site-specific dissociation of singly protonated phosphopeptides-
dc.title.alternativeObservation of phosphorylation site-specific dissociation of singly protonated phosphopeptides-
dc.typeArticle-
dc.citation.titleJournal of American Society for Mass Spectrometry-
dc.citation.number1-
dc.citation.endPage59-
dc.citation.startPage53-
dc.citation.volume21-
dc.contributor.affiliatedAuthorJeong Hee Moon-
dc.contributor.alternativeName신영식-
dc.contributor.alternativeName문정희-
dc.contributor.alternativeName김명수-
dc.identifier.bibliographicCitationJournal of American Society for Mass Spectrometry, vol. 21, no. 1, pp. 53-59-
dc.identifier.doi10.1016/j.jasms.2009.09.003-
dc.description.journalClassY-
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Division of Bio Technology Innovation > Core Research Facility & Analysis Center > 1. Journal Articles
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