SIMULATION OF A PROTEIN CRYSTAL AT CONSTANT-PRESSURE

Constant pressure and temperature molecular dynamics techniques have b een employed to investigate the structure of two unit cells of a hydra ted bovine trypsin inhibitor type I crystal at T = 300 K and P = 0.1 M Pa. The simulations carried out with two different force fields and in cluding full long-range electrostatics showed small deviations from th e experimental structural results. This confirms previous calculations done at constant volume on a smaller sample. Our simulations have als o shown differences in the water diffusion results obtained for the tw o force fields.