Higher-energy C-trap dissociation for peptide modification analysis

Nat Methods. 2007 Sep;4(9):709-12. doi: 10.1038/nmeth1060. Epub 2007 Aug 26.


Peptide sequencing is the basis of mass spectrometry-driven proteomics. Here we show that in the linear ion trap-orbitrap mass spectrometer (LTQ Orbitrap) peptide ions can be efficiently fragmented by high-accuracy and full-mass-range tandem mass spectrometry (MS/MS) via higher-energy C-trap dissociation (HCD). Immonium ions generated via HCD pinpoint modifications such as phosphotyrosine with very high confidence. Additionally we show that an added octopole collision cell facilitates de novo sequencing.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Mass Spectrometry / instrumentation
  • Mass Spectrometry / methods*
  • Peptide Fragments / chemistry*
  • Protein Conformation
  • Proteomics / instrumentation
  • Proteomics / methods*
  • Tandem Mass Spectrometry / instrumentation
  • Tandem Mass Spectrometry / methods*


  • Peptide Fragments