Literature DB >> 17721543

Higher-energy C-trap dissociation for peptide modification analysis.

Jesper V Olsen1, 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.

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Year:  2007        PMID： 17721543     DOI： 10.1038/nmeth1060

Source DB:  PubMed          Journal:  Nat Methods        ISSN： 1548-7091            Impact factor:   28.547


  326 in total

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Journal:  J Am Soc Mass Spectrom       Date:  2017-07-18       Impact factor: 3.109
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