Collision induced dissociations of deprotonated peptides: Dipeptides containing phenylalanine, tyrosine, histidine and tryptophan
โ Scribed by Russell J. Waugh; John H. Bowie; Roger N. Hayes
- Publisher
- Elsevier Science
- Year
- 1991
- Tongue
- English
- Weight
- 741 KB
- Volume
- 107
- Category
- Article
- ISSN
- 0168-1176
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๐ SIMILAR VOLUMES
## Abstract Deprotonated dipeptides, on collisional activation, fragment by the characteristic process NH~2~CH(R^1^) CONHCH(R^2^)CO~2~^โ^ โ NH~2~^โ^C(R^1^)CONHCH(R^2^)CO~2~H โ ^โ^NHCH(R^2^)CO~2~H + NH~2~C(R^1^)๏ฃพC๏ฃพO, when R^1^ and R^2^ = H or alkyl. However, when one of the constituent amino acids i
The characteristic coUisionLinduced dissociations of (M -HI-ions of dipeptides and tripeptides involve proton transfer to the carboxylate centre as a prelude to fragmentation. Dipeptides show the process + NH,C(R')=C=O (R = H or alkyl) while tripeptides show the analogous processes NH,CH(R')CONHCH(R
The characteristic absorption spectra of aromatic amino acids between 240 and 310 nm were used to identify tryptophan, tryosine, and phenylalanine-containing peptides. In acidic solution, the absorption spectra of these amino acids exhibit minima or maxima at 255, 270, and 286 nm. Based on these cha