In an attempt to understand the mechanisms of protein adsorption at the solid-liquid interface, we have calculated the interaction potential energy between the protein and the polymer surface by a computer simulation approach. The adsorption of four proteins--lysozyme, trypsin, immunoglobulin Fab, and hemoglobin--on five polymer surfaces was examined. The model polymers used for the calculation were polystyrene, polyethylene, polypropylene, poly(hydroxyethyl methacrylate), and poly(vinyl alcohol). All possible orientations of the protein on the polymer surfaces were simulated and the corresponding interaction energies for the initial contact stage of protein adsorption were calculated. In the calculation of interaction energies, the hydrophobic interaction was not treated explicitly owing to the difficulty in the theoretical treatment. The results showed that the interaction energy was dependent on the orientation of the protein on the polymer surfaces. The energy varied from -850 to +600 kJ/mol with an average of about -155 kJ/mol. The interaction energy was also dependent on the type of polymer. The average interaction energies of the four proteins with poly(vinyl alcohol) were always lower than those with the other polymers. The interaction energy was not dependent on the protein size. It was found that the dispersion attraction played the major role in protein adsorption on neutral polymer surfaces.