Characterization and diagnostic value of amino acid side chain neutral losses following electron-transfer dissociation

J Am Soc Mass Spectrom. 2011 Feb;22(2):255-64. doi: 10.1007/s13361-010-0029-0. Epub 2011 Jan 27.

Abstract

Using a large set of high mass accuracy and resolution ETD tandem mass spectra, we characterized ETD-induced neutral losses. From these data we deduced the chemical formula for 20 of these losses. Many of them have been previously observed in electron-capture dissociation (ECD) spectra, such as losses of the side chains of arginine, aspartic acid, glutamic acid, glutamine, asparagine, leucine, histidine, and carbamidomethylated cysteine residues. With this information, we examined the diagnostic value of these amino acid-specific losses. Among 1285 peptide-spectrum matches, 92.5% have agreement between neutral loss-derived peptide amino acid composition and the peptide sequences. Moreover, we show that peptides can be uniquely identified by using only the accurate precursor mass and amino acid composition based on neutral losses; the median number of sequence candidates from an accurate mass query is reduced from 21 to 8 by adding side chain loss information. Besides increasing confidence in peptide identification, our findings suggest the potential use of these diagnostic losses in ETD spectra to improve false discovery rate estimation and to enhance the performance of scoring functions in database search algorithms.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acids / chemistry*
  • Amino Acids / metabolism
  • Cations / chemistry
  • Cell Extracts
  • Databases, Protein
  • Electrons
  • Embryonic Stem Cells
  • Humans
  • Metalloendopeptidases / metabolism
  • Peptide Fragments / chemistry*
  • Peptide Fragments / metabolism
  • Tandem Mass Spectrometry / methods*

Substances

  • Amino Acids
  • Cations
  • Cell Extracts
  • Peptide Fragments
  • Metalloendopeptidases
  • peptidyl-Lys metalloendopeptidase