Higher-energy C-trap dissociation for peptide modification analysis

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Higher-energy C-trap dissociation for peptide modification analysis. / Olsen, Jesper Velgaard; Macek, Boris; Lange, Oliver; Makarov, Alexander; Horning, Stevan; Mann, Matthias.

In: Nature Methods, Vol. 4, No. 9, 2007, p. 709-12.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Olsen, JV, Macek, B, Lange, O, Makarov, A, Horning, S & Mann, M 2007, 'Higher-energy C-trap dissociation for peptide modification analysis', Nature Methods, vol. 4, no. 9, pp. 709-12. https://doi.org/10.1038/nmeth1060

APA

Olsen, J. V., Macek, B., Lange, O., Makarov, A., Horning, S., & Mann, M. (2007). Higher-energy C-trap dissociation for peptide modification analysis. Nature Methods, 4(9), 709-12. https://doi.org/10.1038/nmeth1060

Vancouver

Olsen JV, Macek B, Lange O, Makarov A, Horning S, Mann M. Higher-energy C-trap dissociation for peptide modification analysis. Nature Methods. 2007;4(9):709-12. https://doi.org/10.1038/nmeth1060

Author

Olsen, Jesper Velgaard ; Macek, Boris ; Lange, Oliver ; Makarov, Alexander ; Horning, Stevan ; Mann, Matthias. / Higher-energy C-trap dissociation for peptide modification analysis. In: Nature Methods. 2007 ; Vol. 4, No. 9. pp. 709-12.

Bibtex

@article{1e1c8a6c02844a5b83180bfc7b4f15f2,
title = "Higher-energy C-trap dissociation for peptide modification analysis",
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.",
author = "Olsen, {Jesper Velgaard} and Boris Macek and Oliver Lange and Alexander Makarov and Stevan Horning and Matthias Mann",
note = "Keywords: Mass Spectrometry; Peptide Fragments; Protein Conformation; Proteomics; Tandem Mass Spectrometry",
year = "2007",
doi = "10.1038/nmeth1060",
language = "English",
volume = "4",
pages = "709--12",
journal = "Nature Methods",
issn = "1548-7091",
publisher = "nature publishing group",
number = "9",

}

RIS

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

VL - 4

SP - 709

EP - 712

JO - Nature Methods

JF - Nature Methods

SN - 1548-7091

IS - 9

ER -

ID: 46461199