Hydrophobic Interactions in Aqueous Osmolyte Solutions: Thermodynamics of Solvation and Implication on Protein Stability.

ABSTRACT: The effect of cosolvents urea and trimethylamine-N-oxide (TMAO) on hydrophobic association mechanisms is investigated by employing molecular dynamics simulations and free energy calculations. Three nonpolar moieties are used to model the hydrophobic interactions: n-hexane nC₆H₁₄, neopentane C₅H₁₂, and cyclohexane cC₆H₁₂. These hydrophobic model systems are subsequently immersed in four different solvent models with varied composition: pure water, aqueous urea, aqueous TMAO, and mixed urea-TMAO ternary solution. The solute-solute potentials of mean force (PMF), solute-water, and solute-cosolvent distribution functions are reported. Both urea and TMAO are found to have only moderate effects on hydrophobic

SUBMITTER: Dongmo Foumthuim CJ 

PROVIDER: S-EPMC12128031 | biostudies-literature | 2025 May

REPOSITORIES: biostudies-literature