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Role of coulomb energy in promoting collisionally activated dissociation of multiply charged peptides formed by electrospray ionization
Author(s) -
Ishikawa Keiichiro,
Nishimura Toshihide,
Koga Yoshinori,
Niwa Yoshio
Publication year - 1994
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.1290081205
Subject(s) - chemistry , fragmentation (computing) , electrospray ionization , dissociation (chemistry) , tandem mass spectrometry , ionization , quadrupole , intramolecular force , mass spectrometry , coulomb , collision induced dissociation , tandem , electrospray , analytical chemistry (journal) , atomic physics , ion , stereochemistry , chromatography , organic chemistry , physics , materials science , quantum mechanics , computer science , electron , composite material , operating system
Electrospray ionization tandem quadrupole mass spectrometry has been applied to a series of lysine‐substituted octaalanines and some naturally occurring peptides containing more than two basic amino acid residues. Unusually high fragmentation efficiency along with site‐specific cleavages at the outer side of and remote from basic residues were observed for collisionally activated dissociation spectra of multiply charged peptides (MCP) with basic residues in close proximity. It was suggested that Coulomb energy (CE) rather than Coulomb repulsion (CR) was responsible for promoting fragmentation of the MCP studied. A possible fragmentation mechanism of MCP is proposed, in which the conversion of CE into internal vibrational energy was brought about by intramolecular proton migration in the presence of CR between charged sites.