Surface tension kinetics exhibited by the wild type and selected stability mutants of T4 lysozyme at the air-water interface were monitored with DuNouy tensiometry. Mutant lysozymes were produced by substitution of the isoleucine at position 3 with cysteine, leucine, glycine, and tryptophan. Each substitution resulted in an altered structural stability quantified by a change in the free energy of unfolding. Surface pressure kinetics were compared to the kinetic model evolving from a simple model for protein adsorption. This model allowed for parallel, irreversible adsorption into two states directly from solution, where state 2 molecules were more tightly bound to the surface and occupied greater interfacial area than state 1 molecules. Moreover, the model allowed state 2 molecules to increase spreading pressure more than state 1 molecules occupying the same interfacial area. The model indicated that less stable variants of T4 lysozyme have a greater tendency to adsorb in state 2, and state 2 molecules increase spreading pressure more than state 1 molecules occupying the same interfacial area. While agreement between the model and experimental data was very good at low concentration, these results suggest that a more comprehensive two-state model should account for the influence of surface coverage on the adsorption rate constants.