Lermyte, F, Łącki, MK, Valkenborg, D et al. (2 more authors) (2017) Conformational Space and Stability of ETD Charge Reduction Products of Ubiquitin. Journal of the American Society for Mass Spectrometry, 28 (1). pp. 69-76. ISSN 1044-0305
Abstract
Owing to its versatility, electron transfer dissociation (ETD) has become one of the most commonly utilized fragmentation techniques in both native and non-native top-down mass spectrometry. However, several competing reactions—primarily different forms of charge reduction—occur under ETD conditions, as evidenced by the distorted isotope patterns usually observed. In this work, we analyze these isotope patterns to compare the stability of nondissociative electron transfer (ETnoD) products, specifically noncovalent c/z fragment complexes, across a range of ubiquitin conformational states. Using ion mobility, we find that more extended states are more prone to fragment release. We obtain evidence that for a given charge state, populations of ubiquitin ions formed either directly by electrospray ionization or through collapse of more extended states upon charge reduction, span a similar range of collision cross-sections. Products of gas-phase collapse are, however, less stabilized towards unfolding than the native conformation, indicating that the ions retain a memory of previous conformational states. Furthermore, this collapse of charge-reduced ions is promoted if the ions are ‘preheated’ using collisional activation, with possible implications for the kinetics of gas-phase compaction.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2016, American Society for Mass Spectrometry. This is an author produced version of a paper published in Journal of The American Society for Mass Spectrometry. The final publication is available at Springer via https://doi.org/10.1007/s13361-016-1444-7. Uploaded in accordance with the publisher's self-archiving policy. |
Keywords: | ETD; PTR; Charge reduction; Ion mobility; Protein conformation; Ubiquitin |
Dates: |
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Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Biological Sciences (Leeds) > School of Biomedical Sciences (Leeds) |
Depositing User: | Symplectic Publications |
Date Deposited: | 29 Sep 2016 12:36 |
Last Modified: | 10 Aug 2017 04:07 |
Published Version: | https://doi.org/10.1007/s13361-016-1444-7 |
Status: | Published |
Publisher: | Springer Verlag |
Identification Number: | 10.1007/s13361-016-1444-7 |
Related URLs: | |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:105282 |