دورية أكاديمية
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: | Kaldmäe, Margit, Österlund, Nicklas, Lianoudaki, Danai, Sahin, Cagla, Bergman, Peter, Nyman, Tomas, Kronqvist, Nina, Ilag, Leopold L., Allison, Timothy M., Marklund, Erik, Landreh, Michael |
| بيانات النشر: | Uppsala universitet, Biokemi Karolinska Inst, Dept Microbiol Tumor & Cell Biol, Sci Life Lab, S-17165 Stockholm, Sweden Stockholm Univ, Dept Biochem & Biophys, S-10691 Stockholm, Sweden;Stockholm Univ, Dept Environm Sci & Analyt Chem, S-10691 Stockholm, Sweden Karolinska Inst, Dept Lab Med, Div Clin Microbiol, S-14186 Huddinge, Sweden Karolinska Inst, Dept Med Biochem & Biophys, Prot Sci Facil, S-17165 Stockholm, Sweden Karolinska Inst, Dept Neurobiol Care Sci & Soc NVS, Div Neurogeriatr, S-14183 Huddinge, Sweden Stockholm Univ, Dept Environm Sci & Analyt Chem, S-10691 Stockholm, Sweden Univ Canterbury, Biomol Interact Ctr, Christchurch 8140, New Zealand;Univ Canterbury, Sch Phys & Chem Sci, Christchurch 8140, New Zealand SPRINGER |
| سنة النشر: | 2019 |
| المجموعة: | Uppsala University: Publications (DiVA) |
| مصطلحات موضوعية: | Charge reduction, Protein structure, Native mass spectrometry, Gas-phase basicity, Biophysics, Biofysik |
| 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. |
| نوع الوثيقة: | article in journal/newspaper |
| وصف الملف: | application/pdf |
| اللغة: | English |
| ردمك: | 978-0-00-478080-1 0-00-478080-9 |
| العلاقة: | Journal of the American Society for Mass Spectrometry, 1044-0305, 2019, 30:8, s. 1385-1388; http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-392569Test; PMID 31286443; ISI:000478080900006 |
| DOI: | 10.1007/s13361-019-02177-8 |
| الإتاحة: | https://doi.org/10.1007/s13361-019-02177-8Test http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-392569Test |
| حقوق: | info:eu-repo/semantics/openAccess |
| رقم الانضمام: | edsbas.483E6E1E |
| قاعدة البيانات: | BASE |
| ردمك: | 9780004780801 0004780809 |
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| DOI: | 10.1007/s13361-019-02177-8 |