Higher-energy C-trap dissociation for peptide modification analysis

TY - JOUR

T1 - Higher-energy C-trap dissociation for peptide modification analysis

AU - Olsen, Jesper Velgaard

AU - Macek, Boris

AU - Lange, Oliver

AU - Makarov, Alexander

AU - Horning, Stevan

AU - Mann, Matthias

N1 - Keywords: Mass Spectrometry; Peptide Fragments; Protein Conformation; Proteomics; Tandem Mass Spectrometry

PY - 2007

Y1 - 2007

N2 - 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.

AB - 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.

U2 - 10.1038/nmeth1060

DO - 10.1038/nmeth1060

M3 - Journal article

C2 - 17721543

SN - 1548-7091

VL - 4

SP - 709

EP - 712

JO - Nature Methods

JF - Nature Methods

IS - 9

ER -