Trimethylamine N-oxide (TMAO) and urea are naturally occurring osmolytes that have opposing effects on proteins: TMAO stabilizes proteins while urea is a denaturant. while the influences of these molecules on proteins are well studied phenomena, the molecular-level mechanism responsible for this behavior is not clear. One popular theory is that, while urea denatures proteins by interacting with them directly, TMAO can stabilize proteins indirectly by its interactions with water instead. Molecular dynamics simulations, making use of Kirkwood-Buff derived force fields, were performed in order to gain better insight into the specific interactions between both TMAO and urea with water. From these simulations, both the structure of water around the two osmolytes and the diffusive and reorientational dynamics of their solutions were calculated. Comparisons to experimental data and implications for their effect on aqueous solutions will be discussed.

Structure-making and breaking: Structure and dynamics of urea and TMAO in water

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