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Molecular determinant of the effects of hydrostatic pressure on protein folding stability

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  • Calvin R. Chen

    (Rensselaer Polytechnic Institute)

  • George I. Makhatadze

    (Rensselaer Polytechnic Institute)

Abstract

Hydrostatic pressure is an important environmental variable that plays an essential role in biological adaptation for many extremophilic organisms (for example, piezophiles). Increase in hydrostatic pressure, much like increase in temperature, perturbs the thermodynamic equilibrium between native and unfolded states of proteins. Experimentally, it has been observed that increase in hydrostatic pressure can both increase and decrease protein stability. These observations suggest that volume changes upon protein unfolding can be both positive and negative. The molecular details of this difference in sign of volume changes have been puzzling the field for the past 50 years. Here we present a comprehensive thermodynamic model that provides in-depth analysis of the contribution of various molecular determinants to the volume changes upon protein unfolding. Comparison with experimental data shows that the model allows quantitative predictions of volume changes upon protein unfolding, thus paving the way to proteome-wide computational comparison of proteins from different extremophilic organisms.

Suggested Citation

  • Calvin R. Chen & George I. Makhatadze, 2017. "Molecular determinant of the effects of hydrostatic pressure on protein folding stability," Nature Communications, Nature, vol. 8(1), pages 1-9, April.
    • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_ncomms14561
    DOI: 10.1038/ncomms14561
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    Cited by:

    1. Alexandre Pozza & François Giraud & Quentin Cece & Marina Casiraghi & Elodie Point & Marjorie Damian & Christel Le Bon & Karine Moncoq & Jean-Louis Banères & Ewen Lescop & Laurent J. Catoire, 2022. "Exploration of the dynamic interplay between lipids and membrane proteins by hydrostatic pressure," Nature Communications, Nature, vol. 13(1), pages 1-16, December.

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