Evaporation of solvent molecules by ultrafast heating: effect on conformation of solvated protein

Using molecular dynamics simulation, we compare two cases of ultrafast heating of a small water droplet containing a solvated protein (echistatin). If the water temperature after irradiation is above the critical temperature, explosive boiling liberates the protein within some 10 ps of its hydration shell, while its temperature remains relatively low. By comparing with the case where the water shell is heated to the same final temperature, but without complete evaporation, we demonstrate that the protein conformation is governed by the hydration shell rather than by the protein temperature. Copyright © 2010 John Wiley & Sons, Ltd.