We evaluated the performance of our parameters by simulating the binding of hevein, a chitin-binding protein, to our PET crystal film (Figure ). Throughout both additive and Drude trajectories, the residues comprising the chitin-binding domain interacted closely with the PET surface. Residues W21, W23 and H35 engaged in sandwich and T-shaped π-π stacking interactions with PET residues (Figure ), while other polar and charged residues transiently interacted with PET residues through water-bridged interactions. Over the course of our additive simulation, the hevein rapidly bound to the PET surface, although the same hydrophobic interactions were more intermittent. In our Drude simulation, however, the chitin-binding domain rearranged itself in the first 30 ns of the simulation, better positioning W21 and W23 to promote interactions with the PET film. Such dynamic events can be drawn from the time series of interaction energies between the hevein and the PET film (Figure ). By the end of the simulations, the Drude systems yielded an interaction energy more than 20 kcal/mol stronger than the additive system, reflecting the role of electronic polarization in dictating such protein-PET binding events.