Molecular function in cellular processes is governed by protein-protein interactions (PPIs) within biological
networks. Selective yet specific association of these protein partners contributes to diverse functionality such as catalysis,
regulation, assembly, immunity, and inhibition in a cell. Therefore, understanding the principles of protein-protein association
has been of immense interest for several decades. We provide an overview of the experimental methods used to
determine PPIs and the key databases archiving this information. Structural and functional information of existing protein
complexes confers knowledge on the principles of PPI, based on which a classification scheme for PPIs is then introduced.
Obtaining high-quality non-redundant datasets of protein complexes for interaction characterisation is an essential
step towards deciphering their underlying binding principles. Analysis of physicochemical features and their documentation
has enhanced our understanding of the molecular basis of protein-protein association. We describe the diverse
datasets created/collected by various groups and their key findings inferring distinguishing features. The currently available
interface databases and prediction servers have also been compiled.
Keywords: Binding sites, interface features, prediction, protein complexes, protein-protein interactions.
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