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How osmolytes counteract pressure denaturation on a molecular scale

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JournalChemPhysChem
DateAccepted/In press - 26 May 2017
DateE-pub ahead of print - 5 Jul 2017
DatePublished (current) - 18 Aug 2017
Issue number16
Volume18
Number of pages8
Pages (from-to)2243–2249
Early online date5/07/17
Original languageEnglish

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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