Conformational changes of proteins at an interface induced by a supported planar phosphatidic acid monolayer

Conformational changes of two types of proteins, water-soluble proteins (BSA and myoglobin) and membrane-associated protein (cytochrome c), induced by a negatively charged supported planar phospholipid monolayer were studied. The water-soluble proteins lost most of their ordered secondary structure and formed a random conformation in the initial stage of adsorption, and but in the later stage they retained more of the alpha-helical structure which was their main native secondary structure in solution. The membrane-associated protein, cytochrome c, showed a different conformational change in the adsorption process. In the initial stage, it showed an increase in beta-structures but not random coils. In the later stage, it contained more alpha-helixes than that in solution.