Here, to evaluate and quantify the homogeneity of localizations of proteins at the interface, we introduce a quantitative analysis framework based on calculating the relative position distribution (RPD), which represents a histogram of distances between all super-resolved localization coordinates within a specific object . In a recent application of RPD called pattern extraction from relative positions of localizations (PERPL), the authors analyzed the expected 8-fold symmetry of nuclear pore complexes . We extend RPD and PERPL to assess the level of heterogeneity of randomly adsorbed proteins at interfaces. In particular, we quantify distributions obtained in the presence of phosvitin and additional protein emulsifiers. For this purpose, we prepared binary and ternary model systems of mayonnaise. The binary model system comprised of isolated phosvitin and SDS, and the ternary systems were stabilized by phospholipids, SDS and either isolated phosvitin or apoB introduced via LDL. In the ternary phospholipids/SDS/phosvitin emulsion, the phospholipid was added in the form of phosphatidylcholine (PC). In the ternary phospholipid/apoB/SDS emulsions, LDL was used as a vehicle to introduce both apoB and phospholipids, that latter also mainly in the form of PC.