Higher-energy C-trap dissociation for peptide modification analysis

Research output: Contribution to journalJournal articleResearchpeer-review

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.
Original languageEnglish
JournalNature Methods
Volume4
Issue number9
Pages (from-to)709-12
Number of pages3
ISSN1548-7091
DOIs
Publication statusPublished - 2007
Externally publishedYes

Bibliographical note

Keywords: Mass Spectrometry; Peptide Fragments; Protein Conformation; Proteomics; Tandem Mass Spectrometry

ID: 46461199