Projects per year
Abstract
Native mass spectrometry seeks to probe noncovalent protein interactions in terms of protein quaternary structure, protein–protein and protein–ligand complexes. The ultimate goal is to link the understanding of protein interactions to the protein environment by visualizing the spatial distribution of noncovalent protein interactions within tissue. Previously, we have shown that noncovalently bound protein complexes can be directly probed via liquid extraction surface analysis from dried blood spot samples, where hemoglobin is highly abundant. Here, we show that the intact hemoglobin complex can be sampled directly from thin tissue sections of mouse liver and correlated to a visible vascular feature, paving the way for native mass spectrometry imaging.
Original language | English |
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Pages (from-to) | 606-9 |
Journal | Analytical Chemistry |
Volume | 88 |
Issue number | 1 |
Early online date | 6 Dec 2015 |
DOIs | |
Publication status | Published - Jan 2016 |
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Dive into the research topics of 'Direct Tissue Profiling of Protein Complexes: Toward Native Mass Spectrometry Imaging'. Together they form a unique fingerprint.Projects
- 1 Finished
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Chemistry at Birmingham: a Response to the EPSRC Call: Core Capability for Chemistry Research
Simpkins, N., Anderson, P., Britton, M., Bunch, J., Preece, J. & Slater, P.
Engineering & Physical Science Research Council
1/01/13 → 31/03/13
Project: Research
Datasets
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Direct Tissue Profiling of Protein Complexes: Toward Native Mass Spectrometry Imaging
Cooper, H. (Creator), University of Birmingham, 2015
DOI: 10.25500/eData.bham.00000157
Dataset