Model and Experimental Isotherms of Soluble Proteins at water sur faces

수용성 단백질의 계면상 등온곡선의 모델과 실험적 규명

A surface equation of state for globular proteins at air-water interface accounting for the molecular structure, segment-segment, segment-solvent, and electrostatic interactions was proposed and compared to C-14 isotope experiments. This lattice model comprised a simplifying assumption that all adsorbed segments are in the form of trains. The number of segment adsorbed per molecule in case of bovine serum albumin linearly depended on the surface concentration whereas the lysozyme segments adsorbed at the interface were independent of surface concentration. The segment-solvent(water) interaction for both of proteins were found to be unfavorable owing to the proteins unfolding. From comparison of model computation and experimental data, BSA unfolded more than lysozyne because of the larger surface area of contact.