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Gln‐Gly cleavage: a dominant dissociation site in the fragmentation of protonated peptides
Author(s) -
Jonsson Andreas P.,
Bergman Tomas,
Jörnvall Hans,
Griffiths William J.
Publication year - 2001
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.289
Subject(s) - chemistry , peptide , protonation , amino acid , dissociation (chemistry) , cleavage (geology) , fragmentation (computing) , mass spectrometry , peptide sequence , stereochemistry , peptide bond , tandem mass spectrometry , combinatorial chemistry , biochemistry , chromatography , organic chemistry , ion , geotechnical engineering , fracture (geology) , computer science , engineering , gene , operating system
An understanding of the gas‐phase dissociation of protonated peptides within the mass spectrometer is essential for automated high‐throughput protein identification. In this communication we describe a facile cleavage of the Gln‐Gly peptide bond under low‐collisional energy conditions. A variety of synthetic peptides have been analysed where key amino acids have been substituted within the sequence PQGPPQQGGR, which is a consensus repeat present in the tryptic peptides of acidic proline‐rich protein 1 (PRP‐1). The collision‐induced dissociation spectra obtained from the PRP‐1 tryptic peptides and the synthetic peptides indicate that facile Gln‐Gly cleavage occurs when an X‐Gln‐Gly‐Y sequence is present in a peptide, where X is any amino acid and Y any amino acid other than Gly. Copyright © 2001 John Wiley & Sons, Ltd.