Issue 12, 2021

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.

Graphical abstract: Ion mobility-mass spectrometry shows stepwise protein unfolding under alkaline conditions

Supplementary files

Article information

Article type
Communication
Submitted
15 Dec 2020
Accepted
06 Jan 2021
First published
06 Jan 2021

Chem. Commun., 2021,57, 1450-1453

Ion mobility-mass spectrometry shows stepwise protein unfolding under alkaline conditions

C. Sahin, N. Österlund, A. Leppert, J. Johansson, E. G. Marklund, J. L. P. Benesch, L. L. Ilag, T. M. Allison and M. Landreh, Chem. Commun., 2021, 57, 1450 DOI: 10.1039/D0CC08135C

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