Higher-energy C-trap dissociation for peptide modification analysis

被引：715

作者：

Olsen, Jesper V.

Macek, Boris

Lange, Oliver

Makarov, Alexander

Horning, Stevan

Mann, Matthias

机构：

[1] Thermo Fisher Sci GmbH, D-28199 Bremen, Germany

[2] Max Planck Inst Biochem, Dept Proteom & Signal Transduc, D-82131 Martinsried, Germany

来源：

NATURE METHODS | 2007年 / 4卷 / 09期

关键词：

D O I：

10.1038/NMETH1060

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：709 / 712

页数：4

共 16 条

[11]

Perkins DN, 1999, ELECTROPHORESIS, V20, P3551, DOI 10.1002/(SICI)1522-2683(19991201)20:18<3551::AID-ELPS3551>3.0.CO

[12]

2-2

[13] A two-dimensional quadrupole ion trap mass spectrometer [J].