Shimizu, Seishi orcid.org/0000-0002-7853-1683 and Smith, Paul E (2017) How osmolytes counteract pressure denaturation on a molecular scale. ChemPhysChem. 2243–2249. ISSN 1439-4235
Abstract
Life in the deep sea exposes enzymes to high hydrostatic pressure which decreases their stability. For survival, deep sea organisms tend to accumulate various osmolytes, most notably trimethylamine N-oxide (TMAO) used by fish, to counteract pressure denaturation. Yet, exactly how they work still remains unclear. Here, we use a rigorous statistical thermodynamics approach to clarify the mechanism of osmoprotection. We show that the weak, non-specific, and dynamic interactions of water and osmolytes with proteins can be characterized only statistically, and that the competition between protein-osmolyte and protein-water interactions is crucial in determining conformational stability. Osmoprotection is driven by a stronger exclusion of osmolytes from the denatured protein than from the native conformation, and the water distribution has no significant effect on these changes for low osmolyte concentrations.
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2017 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim. This is an author-produced version of the published paper. Uploaded in accordance with the publisher’s self-archiving policy. Further copying may not be permitted; contact the publisher for details |
Dates: |
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Institution: | The University of York |
Academic Units: | The University of York > Faculty of Sciences (York) > Chemistry (York) |
Depositing User: | Pure (York) |
Date Deposited: | 10 Jul 2017 15:00 |
Last Modified: | 06 Dec 2023 11:52 |
Published Version: | https://doi.org/10.1002/cphc.201700503 |
Status: | Published |
Refereed: | Yes |
Identification Number: | https://doi.org/10.1002/cphc.201700503 |
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