ArticleJournal of the American Chemical Society2012
Tyrosine deprotonation yields abundant and selective backbone cleavage in peptide anions upon negative electron transfer dissociation and ultraviolet photodissociation.
Article in Journal of the American Chemical Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
5 citing papers in PubMed.
- The Role of Electron Transfer Dissociation in Modern Proteomics.Analytical chemistry · 2018Review
- Integration of electrochemistry with ultra-performance liquid chromatography/mass spectrometry.European journal of mass spectrometry (Chichester, England) · 2015Article
- Photodissociation mass spectrometry: new tools for characterization of biological molecules.Chemical Society reviews · 2014Review
- Integration of online digestion and electrolytic reduction with mass spectrometry for rapid disulfide-containing protein structural analysis.International journal of mass spectrometry · 2013Article
- The ornithine effect in peptide cation dissociation.Journal of mass spectrometry : JMS · 2013Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Tyrosine deprotonation in peptides yields preferential electron detachment upon NETD or UVPD, resulting in prominent N-Cα bond cleavage N-terminal to the tyrosine residue. UVPD of iodo-tyrosine-modified peptides was used to generate localized radicals on neutral tyrosine side chains by homolytic cleavage of the C-I bond. Subsequent collisional activation of the radical species yielded the same preferential cleavage of the adjacent N-terminal N-Cα bond. LC-MS/MS analysis of a tryptic digest of BSA demonstrated that these cleavages are regularly observed for peptides when using high-pH mobile phases.
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