Effect of cysteic acid position on the negative ion fragmentation of proteolytic derived peptides

Brad J. Williams, Kevin L. Kmiec, William Russell, David H. Russell

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

A study on the effect of cysteic acid position on the types of fragment ions formed by collision-induced dissociation (CID) of [M - H] - ions is presented. Of particular note is the observation of d-type fragment ions for peptides that contain an N-terminal cysteic acid (fixed negative charge) and cleavable amino acid side chains possessing a β-γ carbon-carbon bond. For example, the CID mass spectrum of oxidized cys-kemptide (C oxLRRASLG) [M - H + O 3] - ions contains abundant series of d-type fragment ions, and similar results are observed for oxidized cysteinecontaining ribonuclease A proteolytic peptides. The di fragment ions are assumed to arise by a charge-remote and/or charge-assisted fragmentation mechanism, which both occur at high collision energies and involve consecutive reactions (i.e., the formation of ai ions followed by the elimination of the side chain to form di ions).

Original languageEnglish (US)
Pages (from-to)31-37
Number of pages7
JournalJournal of the American Society for Mass Spectrometry
Volume22
Issue number1
DOIs
StatePublished - Jan 2011
Externally publishedYes

Fingerprint

Cysteic Acid
Negative ions
Ions
Peptides
kemptide
Carbon
Pancreatic Ribonuclease
Peptide Fragments
Observation
Amino Acids

Keywords

  • Cysteic-acid-containing peptides
  • d-type fragment ions
  • MALDI-MS
  • Negative ion tandem mass spectrometry
  • On-target performic acid oxidation
  • Ribonuclease A

ASJC Scopus subject areas

  • Structural Biology
  • Spectroscopy

Cite this

Effect of cysteic acid position on the negative ion fragmentation of proteolytic derived peptides. / Williams, Brad J.; Kmiec, Kevin L.; Russell, William; Russell, David H.

In: Journal of the American Society for Mass Spectrometry, Vol. 22, No. 1, 01.2011, p. 31-37.

Research output: Contribution to journalArticle

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