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Revision with unchanged content. In the past years protein-protein interactions have gained a strong interest in the fields of pharmacy, medicine, biology, and bioinformatics. In this book, statistical information on protein-protein interactions are computationally collected and analyzed. Characteristic properties are determined and their predictability estimated. Therefore, the results from a common docking approach are re-evaluated with the collected information to discriminate structures with high yet biologically meaningless geometric complementarity at the interface region from the near native structures. The results show that although there is a noticeable improvement in the predictability after applying statistical information, the overall accuracy is still low. To find other more specific properties, transient and permanent complexes were compared to each other. The lack of data led to an extensive search for more suitable structural data and the development of an extensive database. This database was ultimately used to retrieve a large number of protein properties that were automatically analyzed for their separation precision. A high accuracy was obtained in separating transient and permanent interactions based on the combination of only four properties. Combining this information with common docking approaches based on geometrical complementarity may lead to satisfying sensitivities.