By the same authors

From the same journal

How osmolytes counteract pressure denaturation on a molecular scale

Research output: Contribution to journalArticle

Full text download(s)

Published copy (DOI)



Publication details

DateAccepted/In press - 26 May 2017
DateE-pub ahead of print - 5 Jul 2017
DatePublished (current) - 18 Aug 2017
Issue number16
Number of pages8
Pages (from-to)2243–2249
Early online date5/07/17
Original languageEnglish


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.

Bibliographical note

© 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

Discover related content

Find related publications, people, projects, datasets and more using interactive charts.

View graph of relations