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Review
. 2023 May 5;3(4):319-326.
doi: 10.1016/j.mrl.2023.04.003. eCollection 2023 Nov.

Using NMR-detected hydrogen-deuterium exchange to quantify protein stability in cosolutes, under crowded conditions in vitro and in cells

I-Te Chu  1 , Gary J Pielak  1   2   3   4
Affiliations
Review

Using NMR-detected hydrogen-deuterium exchange to quantify protein stability in cosolutes, under crowded conditions in vitro and in cells

I-Te Chu et al. Magn Reson Lett. .

Abstract

We review the use of nuclear magnetic resonance (NMR) spectroscopy to assess the exchange of amide protons for deuterons (HDX) in efforts to understand how high concentration of cosolutes, especially macromolecules, affect the equilibrium thermodynamics of protein stability. HDX NMR is the only method that can routinely provide such data at the level of individual amino acids. We begin by discussing the properties of the protein systems required to yield equilibrium thermodynamic data and then review publications using osmolytes, sugars, denaturants, synthetic polymers, proteins, cytoplasm and in cells.

Keywords: Amide proton exchange; Cosolutes; Crowding; Equilibrium thermodynamics; Macromolecular; Osmolytes; Protein stability.

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Conflict of interest statement

Gary J. Pielak is an editorial board member of MRL but was not involved in the editorial review or the decision to publish this article. All authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.

Figures

Image 1
Graphical abstract
Fig. 1
Fig. 1
Hydrogen-deuterium exchange (HDX) and local/global unfolding.
See this image and copyright information in PMC

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