A kinetic model for single component protein adsorption which can be readily extended to adsorption from multi-protein solutions was developed, and used to simulate adsorption of site-directed, structural stability mutants of bacteriophage T4 :lysozyme. The model allows for two different adsorbed "states," distinguished by different binding strengths and different occupied areas. The presence of an increasing energy barrier to adsorption was incorporated into the model by formulating the adsorption rate constants as functions of time. Numerical analysis was performed using the Marquardt method. Estimated model parameters were consistent with the effect of structural stability on adsorption. In particular, kinetic parameters were such that adsorption into the more tightly bound, conformationally altered state was favored by less stable variants.