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Collision induced dissociations of deprotonated peptides: Dipeptides containing phenylalanine, tyrosine, histidine and tryptophan

โœ 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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## Abstract Deprotonated dipeptides, on collisional activation, fragment by the characteristic process NH~2~CH(R^1^) CONHCH(R^2^)CO~2~^โˆ’^ โ†’ NH~2~^โˆ’^C(R^1^)CONHCH(R^2^)CO~2~H โ†’ ^โˆ’^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

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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

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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