Premium
Characterization of underivatized tetrapeptides by negative‐ion fast‐atom bombardment mass spectrometry
Author(s) -
Bradford Adrian M.,
Waugh Russell J.,
Bowie John H.
Publication year - 1995
Publication title -
rapid communications in mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.528
H-Index - 136
eISSN - 1097-0231
pISSN - 0951-4198
DOI - 10.1002/rcm.1290090810
Subject(s) - chemistry , tetrapeptide , fast atom bombardment , fragmentation (computing) , peptide , amino acid , stereochemistry , cleavage (geology) , side chain , mass spectrometry , ion , carboxylate , peptide sequence , chromatography , biochemistry , organic chemistry , polymer , geotechnical engineering , fracture (geology) , computer science , engineering , gene , operating system
The [M H] − ions derived from tetrapeptides generally show two different collision‐induced backbone cleavages which allow the determination of the amino acid sequence of the peptide. The first of these involves the formation of the carboxylate anions of either constituent amino acids or fragment peptides. In the second, amino acids or fragment peptides are eliminated as neutrals. There are a number of residues which undergo characteristic sidechain fragmentations irrespective of their position in the tetrapeptide, e.g. Ser, Thr, Cys, Met, Phe and Tyr. However, there are also some residues which, when situated at the C‐terminal end of the peptide, promote pronounced fragmentation at the C‐terminal position which occurs to the exclusion of the normal backbone cleavages. We conclude that the data obtained from these negative‐ion cleavages are analytically useful, and complement those provided by the cognate positive‐ion technique.