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Earlier in this introduction, the diversity of protein function was attributed largely to processes occurring at the interface between solvent and protein. Proteins often interact with other molecules (often called ligands) as semi-rigid bodies; specificity is provided by the shapes of the protein and ligand surfaces and by hydrophobic and electrostatic attractive forces between them. The relative importance of these factors, particularly in protein-protein interactions, is a matter of controversy[Chothia & Janin, 1975]. A brief summary of the most important concepts is presented below.