Ion mobility-mass spectrometry shows stepwise protein unfolding under alkaline conditions
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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.
Original language | English |
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Journal | Chemical Communications |
Volume | 57 |
Issue number | 12 |
Pages (from-to) | 1450-1453 |
Number of pages | 4 |
ISSN | 1359-7345 |
DOIs | |
Publication status | Published - 2021 |
ID: 257658030