The Library
A mechanism for the loss of 60 u from peptides containing an arginine residue at the C-terminus
Tools
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.
Research output not available from this repository.
Request-a-Copy directly from author or use local Library Get it For Me service.
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 | ||||
Official Date: | March 1997 | ||||
Dates: |
|
||||
Volume: | 8 | ||||
Number: | 3 | ||||
Number of Pages: | 9 | ||||
Page Range: | pp. 253-261 | ||||
Publication Status: | Published |
Data sourced from Thomson Reuters' Web of Knowledge
Request changes or add full text files to a record
Repository staff actions (login required)
View Item |