Following our previous study of adsorption of globular lysozyme and BSA, we continue to explore how another globular protein hydrophobin adsorbs at the oil/water interface by neutron reflection. Inter is preferred because we have built technical capability on this instrument. Our specific aims are to (a) determine the actual thickness and volume fraction of globular hydrophobin and (b) the effect of pH on the interfacial distribution. The results will enable us to compare the extent of proteins distributed into the oil region between these globular proteins at the interface. Hydrophobin has a distinct amphiphilic surface and flexibility in its globular structure, it is thus of interest to explore its distribution in the oil region. The results will enable us to answer if all the globular proteins unfold and produce characteristic segment distributions into the oil region.