Journal article
Ion mobility-mass spectrometry shows stepwise protein unfolding under alkaline conditions
- Abstract:
- Although native mass spectrometry is widely applied to monitor chemical or thermal protein denaturation, it is not clear to what extent it can inform about alkali-induced unfolding. Here, we probe the relationship between solution- and gas-phase structures of proteins under alkaline conditions. Native ion mobility-mass spectrometry reveals that globular proteins are destabilized rather than globally unfolded, which is supported by solution studies, providing detailed insights into alkali-induced unfolding events. Our results pave the way for new applications of MS to monitor structures and interactions of proteins at high pH.
- Publication status:
- Published
- Peer review status:
- Peer reviewed
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- Files:
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(Preview, Accepted manuscript, 2.8MB, Terms of use)
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(Preview, Supplementary materials, 2.0MB, Terms of use)
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- Publisher copy:
- 10.1039/d0cc08135c
Authors
- Publisher:
- Royal Society of Chemistry
- Journal:
- Chemical Communications More from this journal
- Volume:
- 57
- Issue:
- 12
- Pages:
- 1450-1453
- Publication date:
- 2021-01-06
- Acceptance date:
- 2021-01-06
- DOI:
- EISSN:
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1364-548X
- ISSN:
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1359-7345
- Language:
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English
- Keywords:
- Pubs id:
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1153041
- Local pid:
-
pubs:1153041
- Deposit date:
-
2021-01-12
Terms of use
- Copyright holder:
- Royal Society of Chemistry
- Copyright date:
- 2021
- Rights statement:
- © The Royal Society of Chemistry.
- Notes:
- This is the accepted manuscript version of the article. The final version is available online from the Royal Society of Chemistry at: https://doi.org/10.1039/D0CC08135C
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