ArticleThe journal of physical chemistry. B2012
Molecular mechanism for the preferential exclusion of TMAO from protein surfaces.
Article in The journal of physical chemistry. B, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 178 citations in OpenAlex.
- Miscompartmentalization of microbiota-derived TMAO is a reversible driver in autism spectrum disorder.iScience · 2026Article
- Characterization of Liquid-Liquid Phase Separation of Companion of Cellulose Synthases under Stress Mimicking Conditions.bioRxiv : the preprint server for biology · 2026Article
- First Hydration Shell Integrity: Key to Protein Stability.Journal of the American Chemical Society · 2026Article
- Article
- Navigating the landscape of protein folding and proteostasis: from molecular chaperones to therapeutic innovations.Signal transduction and targeted therapy · 2025Review
- Static and Dynamic Correlations in Binary and Ternary Mixtures of TMAO, Urea, and Water.The journal of physical chemistry. B · 2025Article
- Hydrophobic Interactions in Aqueous Osmolyte Solutions: Thermodynamics of Solvation and Implication on Protein Stability.The journal of physical chemistry. B · 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
- Diffusiophoresis of Macromolecules within the Framework of Multicomponent Diffusion.Molecules (Basel, Switzerland) · 2024Review
- The variable domain from dynamin-related protein 1 promotes liquid-liquid phase separation that enhances its interaction with cardiolipin-containing membranes.Protein science : a publication of the Protein Society · 2023Article
- TMAO: Protecting proteins from feeling the heat.Biophysical journal · 2023Article
- Trimethylamine N-oxide: role in cell senescence and age-related diseases.European journal of nutrition · 2023Review
- Electronic fluctuation difference between trimethylamine N-oxide and tert-butyl alcohol in water.Scientific reports · 2022Article
- Interactions in Ternary Aqueous Solutions of NMA and Osmolytes-PARAFAC Decomposition of FTIR Spectra Series.International journal of molecular sciences · 2021Article
- Hydration of Simple Model Peptides in Aqueous Osmolyte Solutions.International journal of molecular sciences · 2021Article
- Conformational dynamics of superoxide dismutase (SOD1) in osmolytes: a molecular dynamics simulation study.RSC advances · 2020Article
- Dynamical Model for the Counteracting Effects of TrimethylamineThe journal of physical chemistry. B · 2020Article
- Dynamical Effects of Trimethylamine N-Oxide on Aqueous Solutions of Urea.The journal of physical chemistry. B · 2019Article
- TrimethylamineProceedings of the National Academy of Sciences of the United States of America · 2017Article
- Thermodynamics of Hydrophobic Amino Acids in Solution: A Combined Experimental-Computational Study.The journal of physical chemistry letters · 2017Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Trimethylamine N-oxide (TMAO) is a naturally occurring protecting osmolyte that stabilizes the folded state of proteins and also counteracts the destabilizing effect of urea on protein stability. Experimentally, it has been inferred that TMAO is preferentially excluded from the vicinity of protein surfaces. Here, we combine computer modeling and experimental measurements to gain an understanding of the mechanism of the protecting effect of TMAO on proteins. We have developed an all-atom molecular model for TMAO that captures the exclusion of TMAO from model compounds and protein surfaces, as a consequence of incorporating realistic TMAO-water interactions through osmotic pressure measurements. Osmotic pressure measurements also suggest no significant attraction between urea and TMAO molecules in solution. To obtain an accurate potential for molecular simulations of protein stability in TMAO solutions, we have explored different ways of parametrizing the protein/osmolyte and osmolyte/osmolyte interactions by scaling charges and the strength of Lennard-Jones interactions and carried out equilibrium folding experiments of Trp-cage miniprotein in the presence of TMAO to guide the parametrization. Our calculations suggest a general principle for preferential interaction behavior of cosolvents with protein surfaces--preferentially excluded osmolytes have repulsive self-interaction given by osmotic coefficient φ > 1, while denaturants, in addition to having attractive interactions with the proteins, have favorable self-interaction given by osmotic coefficient φ < 1, to enable preferential accumulation in the vicinity of proteins.
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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.