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Gas-Phase Collisions with Trimethylamine-N-Oxide Enable Activation-Controlled Protein Ion Charge Reduction
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics. Stockholm University, Faculty of Science, Department of Environmental Science and Analytical Chemistry.
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Number of Authors: 112019 (English)In: Journal of the American Society for Mass Spectrometry, ISSN 1044-0305, E-ISSN 1879-1123, Vol. 30, no 8, p. 1385-1388Article in journal (Refereed) Published
Abstract [en]

Modulating protein ion charge is a useful tool for the study of protein folding and interactions by electrospray ionization mass spectrometry. Here, we investigate activation-dependent charge reduction of protein ions with the chemical chaperone trimethylamine-N-oxide (TMAO). Based on experiments carried out on proteins ranging from 4.5 to 35kDa, we find that when combined with collisional activation, TMAO removes approximately 60% of the charges acquired under native conditions. Ion mobility measurements furthermore show that TMAO-mediated charge reduction produces the same end charge state and arrival time distributions for native-like and denatured protein ions. Our results suggest that gas-phase collisions between the protein ions and TMAO result in proton transfer, in line with previous findings for dimethyl- and trimethylamine. By adjusting the energy of the collisions experienced by the ions, it is possible to control the degree of charge reduction, making TMAO a highly dynamic charge reducer that opens new avenues for manipulating protein charge states in ESI-MS and for investigating the relationship between protein charge and conformation.

Place, publisher, year, edition, pages
2019. Vol. 30, no 8, p. 1385-1388
Keywords [en]
Charge reduction, Protein structure, Native mass spectrometry, Gas-phase basicity
National Category
Biological Sciences Chemical Sciences
Identifiers
URN: urn:nbn:se:su:diva-171684DOI: 10.1007/s13361-019-02177-8ISI: 000478080900006PubMedID: 31286443OAI: oai:DiVA.org:su-171684DiVA, id: diva2:1344498
Available from: 2019-08-21 Created: 2019-08-21 Last updated: 2019-08-21Bibliographically approved

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Österlund, NicklasIlag, Leopold L.
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Department of Biochemistry and BiophysicsDepartment of Environmental Science and Analytical Chemistry
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