Higher-energy C-trap dissociation for peptide modification analysis.
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.
Olsen
Jesper V
JV
Department for Proteomics and Signal Transduction, Max Planck Institute for Biochemistry, Am Klopferspitz 18, D-82131 Martinsried, Germany.
Macek
Boris
B
Lange
Oliver
O
Makarov
Alexander
A
Horning
Stevan
S
Mann
Matthias
M
D013058:Mass Spectrometry / Q000295:instrumentation / Q000379:methods*; D010446:Peptide Fragments / Q000737:chemistry*; D011487:Protein Conformation; D040901:Proteomics / Q000295:instrumentation / Q000379:methods*; D053719:Tandem Mass Spectrometry / Q000295:instrumentation / Q000379:methods*
D010446:Peptide Fragments