Seconded from Biotechnology Research Institute, NRC, Montreal, Canada.
Collision-induced dissociations of peptide ions 2. Remote charge-site fragmentations in a tandem, hybrid mass spectrometer†
Article first published online: 8 APR 2005
Copyright © 1989 Heyden & Son Ltd
Rapid Communications in Mass Spectrometry
Volume 3, Issue 2, pages 30–34, February 1989
How to Cite
Alexander, A. J., Thibault, P. and Boyd, R. K. (1989), Collision-induced dissociations of peptide ions 2. Remote charge-site fragmentations in a tandem, hybrid mass spectrometer. Rapid Commun. Mass Spectrom., 3: 30–34. doi: 10.1002/rcm.1290030206
NRCC No: 29761.
- Issue published online: 8 APR 2005
- Article first published online: 8 APR 2005
- Manuscript Accepted: 30 DEC 1988
- Manuscript Received: 13 DEC 1988
Collision-induced dissociation of peptide ions yields „sequence” ions arising from dissociations of the peptide backbone. Recently, Biemann and his collaborators have elucidated fragment ions involving cleavage of all or part of the side-chains, and have characterized them as remote-site fragmentations of the type investigated for other molecular species by Gross et al. The present work reports results of experiments conducted using a tandem, hybrid mass spectrometer, and devoted to investigating whether remote-site fragmentations (including side-chain cleavages for peptide ions) can be observed for collision energies substantially lower than the keV range used previously. It was found that (laboratory-frame) collision energies of at least 200 eV, and preferably greater, are required for the formation of such fragments. At collision energies in this range the transmission efficiency of the qQ assembly is much lower than for the more usual range of a few tens of eV; this drop in transmission efficiency becomes increasingly severe with increasing mass of the precursor.