PROTEIN DYNAMICS AND SOLVATION IN AQUEOUS AND NONAQUEOUS ENVIRONMENTS

Herein we report the results of molecular dynamics simulations of a protein in an organic solution. We present a detailed analysis of the dynamics and structure of both protein and solvent. These results are compared and contrasted with corresponding results from simulations of protein in water. We find that placement of protein in an organic medium results in a dramatically increased hydrogen bond network. We propose that it is this increase in intramolecular hydrogen bond interactions that is responsible for the experimentally observed properties of proteins in organic solvents. Furthermore, on the basis of our results we propose that creation of salt bridges will significantly enhance the thermostability of enzymes in nonaqueous solvents.