Gas-Phase Collisions with Trimethylamine-N-Oxide Enable Activation-Controlled Protein Ion Charge Reduction
| العنوان: | Gas-Phase Collisions with Trimethylamine-N-Oxide Enable Activation-Controlled Protein Ion Charge Reduction |
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| المؤلفون: | Kaldmae, Margit, Österlund, Nicklas, Lianoudaki, Danai, Sahin, Cagla, Bergman, Peter, Nyman, Tomas, Kronqvist, Nina, Ilag, Leopold L., Allison, Timothy M., Marklund, Erik G., Landreh, Michael |
| المصدر: | Journal of the American Society for Mass Spectrometry. 30(8):1385-1388 |
| مصطلحات موضوعية: | Charge reduction, Protein structure, Native mass spectrometry, Gas-phase basicity |
| الوصف: | 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. |
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| الوصول الحر: | https://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-171684Test https://doi.org/10.1007/s13361-019-02177-8Test |
| قاعدة البيانات: | SwePub |
| تدمد: | 10440305 18791123 |
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| DOI: | 10.1007/s13361-019-02177-8 |