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Two-dimensional mass spectrometry for proteomics, a comparative study with cytochromec

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van Agthoven, Maria, Wootton, Christopher, Chiron, Lionel, Coutouly, Marie-Aude, Soulby, Andrew J., Wei, Juan, Barrow, Mark P., Delsuc, Marc-André, Rolando, Christian and O’Connor, Peter B. (2016) Two-dimensional mass spectrometry for proteomics, a comparative study with cytochromec. Analytical Chemistry, 88 (8). pp. 4409-4417. doi:10.1021/acs.analchem.5b04878

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Official URL: http://dx.doi.org/10.1021/acs.analchem.5b04878

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Abstract

Two-dimensional Fourier transform ion cyclotron resonance mass spectrometry (2D FT-ICR MS) allows the correlation between precursor and fragment ions in tandem mass spectrometry without the need to isolate the precursor ion beforehand. 2D FT-ICR MS has been optimized as a data-independent method for the structural analysis of compounds in complex samples. Data processing methods and denoising algorithms have been developed to use it as an analytical tool. In the present study, the capabilities of 2D FT-ICR MS are explored with a tryptic digest of cytochrome c with both ECD and IRMPD as fragmentation modes. The 2D mass spectra showed useful fragmentation patterns of peptides over a dynamic range of almost 400. By using a quadratic calibration, fragment ion peaks could be successfully assigned. The correlation between precursor and fragment ions in the 2D mass spectra was more accurate than in MS/MS spectra after quadrupole isolation, due to the limitations of quadrupole isolation. The use of the second dimension allowed for successful fragment assignment from precursors that were separated by only m/z 0.0156. The resulting cleavage coverage of cytochrome c almost matched data provided by high-resolution FT-ICR MS/MS analysis, but the 2D FT-ICR MS method required only one experimental scan.

Item Type: Journal Article
Divisions: Faculty of Science > Chemistry
Faculty of Science > Physics
Journal or Publication Title: Analytical Chemistry
Publisher: American Chemical Society
ISSN: 0003-2700
Official Date: 19 April 2016
Dates:
DateEvent
19 April 2016Published
18 March 2016Available
18 March 2016Accepted
Volume: 88
Number: 8
Page Range: pp. 4409-4417
DOI: 10.1021/acs.analchem.5b04878
Status: Peer Reviewed
Publication Status: Published
Access rights to Published version: Restricted or Subscription Access

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