Cells are crowded, but proteins are almost always studied in dilute aqueous buffer. We
review the experimental evidence that crowding affects the equilibrium thermodynamics of …

Proteins are marginally stable, and the folding/unfolding equilibrium of proteins in aqueous
solution can easily be altered by the addition of small organic molecules known as …

While the quality of the current CHARMM22/CMAP additive force field for proteins has been
demonstrated in a large number of applications, limitations in the model with respect to the …

Intrinsically disordered proteins (IDPs) are widely distributed across eukaryotic cells, playing
important roles in molecular recognition, molecular assembly, post-translational …

In order to clarify the mechanism of denaturant-induced unfolding of proteins we have
calculated the interactions between hydrophobic and ionic species in aqueous guanidinium …

To explain the large, opposite effects of urea and glycine betaine (GB) on stability of folded
proteins and protein complexes, we quantify and interpret preferential interactions of urea …

Though urea is commonly used to denature proteins, the molecular mechanism of its
denaturing ability is still a subject of considerable debate. Previous molecular dynamics …

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 …

We discuss two methods for calculating Kirkwood–Buff integrals (KBIs) of aqueous cosolvent
solutions from molecular simulations. The first method is based on computing running …

Urea is ubiquitously used as a protein denaturant. To study the structure and energetics of
aqueous urea solutions, we have carried out molecular dynamics simulations for a wide …