ArticleJournal of the American Chemical Society2012
Volume exclusion and H-bonding dominate the thermodynamics and solvation of trimethylamine-N-oxide in aqueous urea.
Article in Journal of the American Chemical Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 82 citations in OpenAlex.
- Static and Dynamic Correlations in Binary and Ternary Mixtures of TMAO, Urea, and Water.The journal of physical chemistry. B · 2025Article
- Solvent accessible surface area-assessed molecular basis of osmolyte-induced protein stability.RSC advances · 2024Article
- Synergistic Solvation as the Enhancement of Local Mixing.The journal of physical chemistry. B · 2024Article
- TMAO: Protecting proteins from feeling the heat.Biophysical journal · 2023Article
- Weighted persistent homology for osmolyte molecular aggregation and hydrogen-bonding network analysis.Scientific reports · 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
- Effects of trimethylamine oxide (TMAO) and loading duration on the shoot tip cryopreservation of loquat (Turkish journal of biology = Turk biyoloji dergisi · 2018Article
- Trimethylamine-N-oxide switches from stabilizing nature: A mechanistic outlook through experimental techniques and molecular dynamics simulation.Scientific reports · 2016Article
- Synergy in protein-osmolyte mixtures.The journal of physical chemistry. B · 2015Article
- Microscopic insights into the protein-stabilizing effect of trimethylamine N-oxide (TMAO).Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Distinctive solvation patterns make renal osmolytes diverse.Biophysical journal · 2013Article
- Compensating effects of urea and trimethylamine-N-oxide on the heteroassociation of α-chymotrypsin and soybean trypsin inhibitor.The journal of physical chemistry. B · 2013Article
- Counteracting chemical chaperone effects on the single-molecule α-synuclein structural landscape.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Molecular mechanism for the preferential exclusion of TMAO from protein surfaces.The journal of physical chemistry. B · 2012Article
Corrections and comments
- Erratum issued
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Trimethylamine-N-oxide (TMAO) and urea represent the extremes among the naturally occurring organic osmolytes in terms of their ability to stabilize/destabilize proteins. Their mixtures are found in nature and have generated interest in terms of both their physiological role and their potential use as additives in various applications (crystallography, drug formulation, etc.). Here we report experimental density and activity coefficient data for aqueous mixtures of TMAO with urea. From these data we derive the thermodynamics and solvation properties of the osmolytes, using Kirkwood-Buff theory. Strong hydrogen-bonding at the TMAO oxygen, combined with volume exclusion, accounts for the thermodynamics and solvation of TMAO in aqueous urea. As a result, TMAO behaves in a manner that is surprisingly similar to that of hard-spheres. There are two mandatory solvation sites. In plain water, these sites are occupied with water molecules, which are seamlessly replaced by urea, in proportion to its volume fraction. We discuss how this result gives an explanation both for the exceptionally strong exclusion of TMAO from peptide groups and for the experimentally observed synergy between urea and TMAO.
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