Structural influences on preferential oxazolone versus diketopiperazine b(2+) ion formation for histidine analogue-containing peptides.

@article{Gucinski2012StructuralIO,
  title={Structural influences on preferential oxazolone versus diketopiperazine b(2+) ion formation for histidine analogue-containing peptides.},
  author={Ashley C Gucinski and Julia Chamot-Rooke and Edith A. T. Nicol and {\'A}rpad́ Somogyi and Vicki H. Wysocki},
  journal={The journal of physical chemistry. A},
  year={2012},
  volume={116 17},
  pages={4296-304}
}
Studies of peptide fragment ion structures are important to aid in the accurate kinetic modeling and prediction of peptide fragmentation pathways for a given sequence. Peptide b(2)(+) ion structures have been of recent interest. While previously studied b(2)(+) ions that contain only aliphatic or simple aromatic residues are oxazolone structures, the HA b(2)(+) ion consists of both oxazolone and diketopiperazine structures. The structures of a series of histidine-analogue-containing Xxx-Ala b(2… CONTINUE READING
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Rapid Commun. Mass Spectrom

  • B. Paizs, S. Suhai
  • J. Mol. Biol
  • 2002

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