ArticleChemphyschem : a European journal of chemical physics and physical chemistry2017
How Osmolytes Counteract Pressure Denaturation on a Molecular Scale.
Article in Chemphyschem : a European journal of chemical physics and physical chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
4 citing papers in PubMed, 18 citations in OpenAlex.
- Calorimetric characterization of the stability and activity of trimethylamine-N-oxide (TMAO) demethylase from Methylocella silvestris BL2.Protein science : a publication of the Protein Society · 2025Article
- Trimethylamine-N-oxide depletes urea in a peptide solvation shell.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- In Silico and In Vitro Studies of Antibacterial Activity of Cow Urine Distillate (CUD).Evidence-based complementary and alternative medicine : eCAM · 2024Article
- The ability of trimethylamine N-oxide to resist pressure induced perturbations to water structure.Communications chemistry · 2022Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
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 used by fish, to counteract pressure denaturation. However, exactly how these osmolytes work remains unclear. Here, a rigorous statistical thermodynamics approach is used to clarify the mechanism of osmoprotection. It is shown that the weak, nonspecific, 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 water distribution has no significant effect on these changes at low osmolyte concentrations.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.