Complex life processes require proteins to be able to transfer specific signals, build multiprotein complexes, control the function of enzymes, and regulate all other cellular activities. Many of these tasks are performed through specific proteinprotein interactions. This is feasible due to the almost unlimited potential for the generation of protein binding sites, unique sites characterized by their shape and surface chemistry. A major research area today is the investigation of the structure, mechanisms, and dynamics of protein-protein interactions. One model system being utilized for basic research into the mechanisms of protein complex formation uses the interactions between TEM1 b-lactamase enzyme (TEM1) and its inhibitor, b-lactamase inhibitor protein (BLIP).