We develop a unified and generally applicable theory of solvation of small and large apolar species in water. In the former, hydrogen bonding of water is hindered yet persists near the solutes. In the latter, hydrogen bonding is depleted, leading to drying of extended apolar surfaces, large forces of attraction, and hysteresis on mesoscopic length scales. The crossover occurs on nanometer length scales, when the local concentration of apolar units is sufficiently high, or when an apolar surface is sufficiently large. Our theory for the crossover has implications concerning the stability of protein assemblies and protein folding.
Protein structures generally consist of favorable folding motifs formed by specific arrangements of secondary structure elements. Similar architectures can be adopted by differe...
Abstract A first‐generation fluctuating charge (FQ) force field to be ultimately applied for protein simulations is presented. The electrostatic model parameters, the atomic har...
Abstract Thermodynamic information can be inferred from static atomic configurations. To model the thermodynamics of carbohydrate binding to proteins accurately, a large binding...
Macromolecular crowding has a profound effect upon biochemical processes in the cell. We have computationally studied the effect of crowding upon protein folding for 12 small do...
We have carried out a natural bond orbital analysis of hydrogen bonding in the water dimer for the near-Hartree–Fock wave function of Popkie, Kistenmacher, and Clementi, extendi...
Social media, news, blog, policy document mentions