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.
Metadata
Item Type: | Article |
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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: | 10 Mar 2025 00:05 |
Published Version: | https://doi.org/10.1002/cphc.201700503 |
Status: | Published |
Refereed: | Yes |
Identification Number: | 10.1002/cphc.201700503 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:118912 |
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