Cellular functions are the result of the coordinated action of groups of proteins interacting in molecular assemblies or pathways. The systematic and unbiased charting of protein-protein networks in a variety of organisms has become an important challenge in systems biology. These protein-protein interaction networks contribute comprehensive cartographies of key pathways or biological processes relevant to health or disease by providing a molecular frame for the interpretation of genetic links. At a structural level protein-protein networks enabled the identification of the sequences, motifs and structural folds involved in the process of molecular recognition. A rapidly growing choice of technologies is available for the global charting of protein-protein interactions. In this review, we focus on recent developments in a suite of methods that enable the purification of protein complexes under native conditions and, in conjunction with protein mass spectrometry, identification of their constituents.
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