Principal Investigator Adam Willard
Water plays a fundamental role in processes that cut across all branches of science. Irrespective of its prevalence, water is particularly interesting because of its unique microscopic structure, which consists of a disordered array of molecules engaged in a three-dimensional hydrogen bonding network. Resolving this picture and how it relates to macroscopic properties has been a problem of long-standing scientific interest. At the interface between liquid water and a disordered substrate (such as the surface of a protein) the microscopic details of interfacial structure reflect a competition between water-water and water-substrate interactions. Variations in the balance between these interactions, along with their effect on the termination of water's three-dimensional hydrogen bonding network account for the large array of observed hydrophilic interfacial structures. This forms the basis for a rich and challenging problem in statistical mechanics.
Research is aimed at providing a statistical mechanical framework for analyzing the molecular structure and dynamics of liquid water interfaces. Specifically, we apply tools from information theory to the analysis of atomistic simulation data as a novel and minimally subjective methodology for quantifying the molecular details of interfacial structure. We apply these tools to investigate protein hydration to explore how heterogeneous surface chemistry and conformational dynamics affect the microscopic properties of the protein's hydration shell.