## Abstract The neutral products arising during the collisionally activated dissociation of protonated oligopeptides (MH^+^) are post‐ionized by collision and detected in neutral fragment‐reionization (^+^N~f~R^+^) mass spectra. For the isomeric tripeptides Ala‐Gly‐Gly, Gly‐Ala‐Gly and Gly‐Gly‐Ala,
Tandem mass spectrometry of peptides: Sequence information based on neutral losses. I—isomeric dipeptides
✍ Scribed by Marcela M. Cordero; Chrys Wesdemiotis
- Publisher
- John Wiley and Sons
- Year
- 1993
- Tongue
- English
- Weight
- 488 KB
- Volume
- 28
- Category
- Article
- ISSN
- 1076-5174
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✦ Synopsis
Abstract
The neutral losses arising on the collisionally activated dissociation (CAD) of protonated dipeptides (MH^+^) are reionized by collision and detected in neutral fragment‐reionization (N~f~R) mass spectra. For the dipeptides investigated, which encompass Ala–Gly/Gly–Ala, Asp–Gly/Gly–Asp, Phe–Gly/Gly–Phe and Trp–Ala/Ala–Trp, the N~f~R spectra of each pair of isomers are distinct and permit the identification of the correct C‐terminal amino acid. The precise structure of this amino acid is elucidated by comparison of the N~f~R spectra with reference collision‐induced dissociative ionization (CIDI) mass spectra of authentic Gly, Ala, Asp, Phe and Trp, acquired from beams of these amino acids formed by dissociation of their proton‐bound dimers.
📜 SIMILAR VOLUMES
## Abstract The neutral species generated during the collisionally activated dissociation (CAD) of the protonated dipeptides Ala–Leu, Ala–Ile, Leu–Ala and Ile–Ala are post‐ionized by collision and detected in neutral fragment‐reionization (^+^N~f~R^+^) mass spectra. These spectra are dominated by f