The adsorption behavior of lysozyme and ribonuclease on nickel powder was studied to elucidate the effects of hydrophobicity, structural stability, and electrostatic forces. The results indicated that the equilibrium between proteins and nickel can be reached in about 20 min and some "overshoot" phenomena in adsorption were found. Maximal adsorption at the IEP, which could result in multilayer adsorption, was also noticed. A reduction in adsorption due to ionic shielding was observed for Cl- and SCN-, while the addition of ethanol promoted adsorption. FT-IR/ATR spectra were used to monitor the conformational changes during the adsorption process.