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Gas-Phase Collisions with Trimethylamine-N-Oxide Enable Activation-Controlled Protein Ion Charge Reduction
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 ca...
Autores principales: | , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer US
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6669196/ https://www.ncbi.nlm.nih.gov/pubmed/31286443 http://dx.doi.org/10.1007/s13361-019-02177-8 |
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author | Kaldmäe, Margit Österlund, Nicklas Lianoudaki, Danai Sahin, Cagla Bergman, Peter Nyman, Tomas Kronqvist, Nina Ilag, Leopold L. Allison, Timothy M. Marklund, Erik G. Landreh, Michael |
author_facet | Kaldmäe, Margit Österlund, Nicklas Lianoudaki, Danai Sahin, Cagla Bergman, Peter Nyman, Tomas Kronqvist, Nina Ilag, Leopold L. Allison, Timothy M. Marklund, Erik G. Landreh, Michael |
author_sort | Kaldmäe, Margit |
collection | PubMed |
description | 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 35 kDa, 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. [Figure: see text] ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1007/s13361-019-02177-8) contains supplementary material, which is available to authorized users. |
format | Online Article Text |
id | pubmed-6669196 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Springer US |
record_format | MEDLINE/PubMed |
spelling | pubmed-66691962019-08-14 Gas-Phase Collisions with Trimethylamine-N-Oxide Enable Activation-Controlled Protein Ion Charge Reduction Kaldmäe, Margit Österlund, Nicklas Lianoudaki, Danai Sahin, Cagla Bergman, Peter Nyman, Tomas Kronqvist, Nina Ilag, Leopold L. Allison, Timothy M. Marklund, Erik G. Landreh, Michael J Am Soc Mass Spectrom Focus: Emerging Investigators: Short Communication 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 35 kDa, 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. [Figure: see text] ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1007/s13361-019-02177-8) contains supplementary material, which is available to authorized users. Springer US 2019-07-08 2019 /pmc/articles/PMC6669196/ /pubmed/31286443 http://dx.doi.org/10.1007/s13361-019-02177-8 Text en © The Author(s) 2019 Open Access This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. |
spellingShingle | Focus: Emerging Investigators: Short Communication Kaldmäe, Margit Österlund, Nicklas Lianoudaki, Danai Sahin, Cagla Bergman, Peter Nyman, Tomas Kronqvist, Nina Ilag, Leopold L. Allison, Timothy M. Marklund, Erik G. Landreh, Michael Gas-Phase Collisions with Trimethylamine-N-Oxide Enable Activation-Controlled Protein Ion Charge Reduction |
title | Gas-Phase Collisions with Trimethylamine-N-Oxide Enable Activation-Controlled Protein Ion Charge Reduction |
title_full | Gas-Phase Collisions with Trimethylamine-N-Oxide Enable Activation-Controlled Protein Ion Charge Reduction |
title_fullStr | Gas-Phase Collisions with Trimethylamine-N-Oxide Enable Activation-Controlled Protein Ion Charge Reduction |
title_full_unstemmed | Gas-Phase Collisions with Trimethylamine-N-Oxide Enable Activation-Controlled Protein Ion Charge Reduction |
title_short | Gas-Phase Collisions with Trimethylamine-N-Oxide Enable Activation-Controlled Protein Ion Charge Reduction |
title_sort | gas-phase collisions with trimethylamine-n-oxide enable activation-controlled protein ion charge reduction |
topic | Focus: Emerging Investigators: Short Communication |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6669196/ https://www.ncbi.nlm.nih.gov/pubmed/31286443 http://dx.doi.org/10.1007/s13361-019-02177-8 |
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