Higher-energy C-trap dissociation for peptide modification analysis View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2007-09

AUTHORS

Jesper V Olsen, Boris Macek, Oliver Lange, Alexander Makarov, Stevan Horning, Matthias Mann

ABSTRACT

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. More... »

PAGES

709-712

References to SciGraph publications

  • 2003-03. Mass spectrometry-based proteomics in NATURE
  • 2004-09. Temporal analysis of phosphotyrosine-dependent signaling networks by quantitative proteomics in NATURE BIOTECHNOLOGY
  • 2002-06. A two-dimensional quadrupole ion trap mass spectrometer in JOURNAL OF THE AMERICAN SOCIETY FOR MASS SPECTROMETRY
  • 2004-09. The abc's (and xyz's) of peptide sequencing in NATURE REVIEWS MOLECULAR CELL BIOLOGY
  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/nmeth1060

    DOI

    http://dx.doi.org/10.1038/nmeth1060

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1043866234

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/17721543


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