A mechanism for the loss of 60 u from peptides containing an arginine residue at the C-terminus
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 1044-0305Full text not available from this repository.
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|
|Number of Pages:||9|
|Page Range:||pp. 253-261|
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