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Gln‐Gly cleavage: a dominant dissociation site in the fragmentation of protonated peptides by Andreas P. Jonsson; Tomas Bergman; Hans Jörnvall; William J. Griffiths is a Chemistry article available to read on EtoBox.

## Abstract 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.

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Author
Andreas P. Jonsson; Tomas Bergman; Hans Jörnvall; William J. Griffiths
Publisher
John Wiley and Sons; Wiley (John Wiley & Sons); John Wiley & Sons Inc.; Wiley (ISSN 0951-4198)
Published
2001
Language
EN
Field
Chemistry (Physical Sciences)