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A mechanism for the loss of 60 u from peptides containing an arginine residue at the C-terminus
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UNSPECIFIED (1997) A mechanism for the loss of 60 u from peptides containing an arginine residue at the C-terminus. JOURNAL OF THE AMERICAN SOCIETY FOR MASS SPECTROMETRY, 8 (3). pp. 253-261. ISSN 1044-0305
Full text not available from this repository.Abstract
The loss of 60 u from protonated peptide ions containing an arginine residue at the C-terminus has been investigated by means of low energy tandem mass spectrometry. The lowest energy conformation of singly charged bradykinin is thought to involve a salt-bridge structure, which may lead to the formation of two isomeric forms. It is thought that one isomer retains the ionizing proton at the C-terminal end of the peptide, leading to the formation of the [b(n-1) + H + OH](+) fragment ion, and the other isomer retains the charge at the N-terminus, leading to the formation of the [M + H - 60](+) fragment ion. It was found that the formation of the [M + H - 60](+) ion occurs only from singly charged precursor ions. In addition, the loss of 60 u occurs from peptides in which the charge is localized at the N-terminus. These results indicate that the mechanism of formation of the [M + H - 60](+) ion may be driven by a charge-remote process. (C) 1997 American Society for Mass Spectrometry.
| Item Type: | Journal Article |
|---|---|
| Subjects: | Q Science > QD Chemistry Q Science > QC Physics |
| Journal or Publication Title: | JOURNAL OF THE AMERICAN SOCIETY FOR MASS SPECTROMETRY |
| Publisher: | ELSEVIER SCIENCE INC |
| ISSN: | 1044-0305 |
| Date: | March 1997 |
| Volume: | 8 |
| Number: | 3 |
| Number of Pages: | 9 |
| Page Range: | pp. 253-261 |
| Publication Status: | Published |
| URI: | http://wrap.warwick.ac.uk/id/eprint/17960 |
Data sourced from Thomson Reuters' Web of Knowledge
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