Publication: Dissociation of the NâCα Bond and Competitive Formation of the [zn â H]â+ and [cn + 2H]+ Product Ions in Radical Peptide Ions Containing Tyrosine and Tryptophan: The Influence of Proton Affinities on Product Formation
All || By Area || By YearTitle | Dissociation of the NâCα Bond and Competitive Formation of the [zn â H]â+ and [cn + 2H]+ Product Ions in Radical Peptide Ions Containing Tyrosine and Tryptophan: The Influence of Proton Affinities on Product Formation | Authors/Editors* | Chi-Kit Siu, Yuyong Ke, Galina Orlova, Alan C. Hopkinson, and K. W. Michael Siu |
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Where published* | Journal of the American Society for Mass Spectrometry |
How published* | Journal |
Year* | 2008 |
Volume | 19 |
Number | |
Pages | 1799-1807 |
Publisher | |
Keywords | |
Link | http://dx.doi.org/10.1016/j.jasms.2008.09.026 |
Abstract |
Dissociations at the NâCï¡ bond of tryptophan and tyrosine residues are the prevalent pathways in the fragmentations of radical cations of tripeptides that contain such as residues. This process involves a proton transfer from the ï¢-carbon of the tryptophan or tyrosine residue to the carbonyl oxygen of the amide group, followed by cleavage of the NâCï¡ bond, generating low-lying proton-bound dimers that dissociate to give each an ionic and a neutral product. Formation of the [zn â H]â+ or [cn + 2H]+ ion is a competition between the two incipient fragments for the proton in a dissociating proton-bound dimer. |
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