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Ion mobility-mass spectrometry shows stepwise protein unfolding under alkaline conditions
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- Sahin, Cagla (author)
- Karolinska Institutet
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- Österlund, Nicklas (author)
- Stockholms universitet,Institutionen för biokemi och biofysik,Institutionen för material- och miljökemi (MMK)
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- Leppert, Axel (author)
- Karolinska Institutet
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- Marklund, Erik G. (author)
- Benesch, Justin L. P. (author)
- Allison, Timothy M. (author)
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- (creator_code:org_t)
- 2021
- 2021
- English.
- In: Chemical Communications. - : Royal Society of Chemistry (RSC). - 1359-7345 .- 1364-548X. ; 57:12, s. 1450-1453
- Journal article (peer-reviewed)
Abstract
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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.
Subject headings
- NATURVETENSKAP -- Kemi (hsv//swe)
- NATURAL SCIENCES -- Chemical Sciences (hsv//eng)
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- ref (subject category)
- art (subject category)
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