Theoretical Studies of Aqueous Solvation of Proteins

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The research described here is to develop theories for aqueous solvation of proteins. Simple continuum solvent models are insufficient to describe phenomena such as hydrogen-bonding, orientation of water dipoles, and interactions involving separations of only a few water layers. The three main objectives of this project are to develop analytic molecular theories of solvation, to use these theories to develop new methods for treating solvent effects in molecular dynamics simulations, and to study the solvation of a specific protein, rubredoxin. While the straightforward approach is to include water molecules in computer simulations of proteins, this becomes impractical as the size or number of proteins and other molecules increases. The approach here is to employ integral equation theories which predict the molecular structure of liquids but with much less computation than simulation methods. These theories can be used to calculate the net forces on the protein due to the solvent. %%% Theories for solvent effects on macromolecules are crucial to developing theoretical methods to probe the structure, dynamics and thermodynamics of biopolymers. Specific, current problems for proteins to which these theories can be applied include folding, enzyme-substrate binding, and electron-transfer in and between proteins.