Nature Methods
- 4, 709 - 712 (2007)
Published online: 26 August 2007; | doi:10.1038/nmeth1060
Higher-energy C-trap dissociation for peptide modification analysisJesper V Olsen1, Boris Macek1, Oliver Lange2, Alexander Makarov2, Stevan Horning2 & Matthias Mann11
Department for Proteomics and Signal Transduction, Max Planck Institute for Biochemistry, Am Klopferspitz 18, D-82131 Martinsried, Germany. 2
Thermo Fisher Scientific (Bremen) GmbH, Hanna-Kunath-Strasse 11, D-28199 Bremen, Germany.
Correspondence should be addressed to Stevan Horning stevan.horning@thermofisher.com or Matthias Mann mmann@biochem.mpg.de 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.
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