Insight into Protein Conformation and Subcharging by DMSO from Native Ion Mobility Mass Spectrometry
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Chan, D., Matak Vinkovic, D., Coyne, A., & Abell, C. (2016). Insight into Protein Conformation and Subcharging by DMSO from Native Ion Mobility Mass Spectrometry. ChemistrySelect, 1 (18), 5686-5690. https://doi.org/10.1002/slct.201601402
Electrospray ionization-mass spectrometry (ESI-MS) interfaced with ion-mobility (IM) spectrometry has enabled the study of protein structure and interactions under native-like conditions. In biological assays, dimethyl sulfoxide (DMSO) is often included as a co-solvent to dissolve organic molecules. While low levels of DMSO are known to reduce the charge of protein ions generated by ESI, the exact mechanism by which this occurs has been debated. In this study, we describe the first application of IM–MS to study the effect of DMSO subcharging on native protein conformation. We find that at low concentrations, DMSO induces modest (1-2 %), but repeatable, reductions in protein collision-cross sections (CCSs) of four different protein complexes, avidin, concanavalin A, alcohol dehydrogenase, and pyruvate kinase, as measured by traveling-wave (TW) IM–MS. Individual protein charge states also experienced compaction in size, suggesting that this effect could not be attributed to the shift of charge state distribution by DMSO alone.
DMSO, electrospray, ion mobility, mass spectrometry, subcharging
Is supplemented by: https://doi.org/10.17863/CAM.5953
D.S.-H. Chan acknowledges the support of the Croucher Foundation and the Cambridge Commonwealth, European and International Trust for receipt of a Croucher Cambridge International Scholarship.
External DOI: https://doi.org/10.1002/slct.201601402
This record's URL: https://www.repository.cam.ac.uk/handle/1810/261722