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Uncoiling collagen : a multidimensional mass spectrometry study
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Simon, H. J., van Agthoven, Maria, Lam, P. Y., Floris, Federico, Chiron, L., Delsuc, M.-A., Rolando, C., Barrow, Mark P. and O'Connor, Peter B. (2016) Uncoiling collagen : a multidimensional mass spectrometry study. The Analyst, 141 (1). pp. 157-165. doi:10.1039/c5an01757b ISSN 1364-5528.
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Official URL: https://doi.org/10.1039/C5AN01757B
Abstract
Mass spectrometry can be used to determine structural information about ions by activating precursors and analysing the resulting series of fragments. Two-dimensional Fourier transform ion cyclotron resonance mass spectrometry (2D FT-ICR MS) is a technique that correlates the mass-to-charge (m/z) ratio of fragment and precursor ions in a single spectrum. 2D FT-ICR MS records the fragmentation of all ions in a sample without the need for isolation. To analyse specific precursors, horizontal cross-sections of the spectrum (fragment ion scans) are taken, providing an alternative to conventional tandem mass spectrometry (MS/MS) experiments. In this work, 2D FT-ICR MS has been used to study the tryptic digest of type I collagen, a large protein. Fragment ion scans have been extracted from the 2D FT-ICR MS spectrum for precursor m/z ratios: 951.81, 850.41, 634.34, and 659.34, and 2D FT-ICR MS spectra are compared with a set of 1D MS/MS spectra using different fragmentation methods. The results show that two-dimensional mass spectrometry excells at MS/MS of complex mixtures, simplifying spectra by eliminating contaminant peaks, and aiding the identification of species in the sample. Currently, with desktop computers, 2D FT-ICR MS is limited by data processing power, a limitation which should be alleviated using cluster parallel computing. In order to explore 2D FT-ICR MS for collagen, with reasonable computing time, the resolution in the fragment ion dimension is limited to 256k data points (compared to 4M data points in 1D MS/MS spectra), but the vertical precursor ion dimension has 4096 lines, so the total data set is 1G data points (4 Gbytes). The fragment ion coverage obtained with a blind, unoptimized 2D FT-ICR MS experiment was lower than conventional MS/MS, but MS/MS information is obtained for all ions in the sample regardless of selection and isolation. Finally, although all 2D FT-ICR MS peak assignments were made with the aid of 1D FT-ICR MS data, these results demonstrate the promise of 2D FT-ICR MS as a technique for studying complex protein digest mixtures.
Item Type: | Journal Article | ||||||
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Subjects: | Q Science > QD Chemistry Q Science > QP Physiology |
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Divisions: | Faculty of Science, Engineering and Medicine > Science > Chemistry | ||||||
SWORD Depositor: | Library Publications Router | ||||||
Library of Congress Subject Headings (LCSH): | Collagen., Mass spectrometry., Chemistry, Organic. | ||||||
Journal or Publication Title: | The Analyst | ||||||
Publisher: | Royal Society of Chemistry (RSC) | ||||||
ISSN: | 1364-5528 | ||||||
Official Date: | 2016 | ||||||
Dates: |
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Volume: | 141 | ||||||
Number: | 1 | ||||||
Page Range: | pp. 157-165 | ||||||
DOI: | 10.1039/c5an01757b | ||||||
Status: | Peer Reviewed | ||||||
Publication Status: | Published | ||||||
Reuse Statement (publisher, data, author rights): | ** From Crossref via Jisc Publications Router. | ||||||
Access rights to Published version: | Open Access (Creative Commons) | ||||||
Date of first compliant deposit: | 29 September 2017 | ||||||
Date of first compliant Open Access: | 2 October 2017 | ||||||
Funder: | Engineering and Physical Sciences Research Council (EPSRC), France. Agence nationale de la recherche (ANR) | ||||||
Grant number: | EP/J000302 |
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