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Title: In Vivo Cross-Linking to Analyze Transient Protein-Protein Interactions. Author: Pertl-Obermeyer H, Obermeyer G. Journal: Methods Mol Biol; 2020; 2139():273-287. PubMed ID: 32462593. Abstract: Cross-linking converts noncovalent interactions between proteins into covalent bonds. The now artificially fused molecules are stable during purification steps (e.g., immunoprecipitation). In combination with a variety of techniques, including Western blotting, mass spectrometry (MS), and bioinformatics, this technology provides improved opportunities for modelling structural details of functional complexes in living cells and protein-protein interaction networks. The presented strategy of immunoaffinity purification and mass spectrometry (AP-MS) coupled with in vivo cross-linking can easily be adapted as a robust workflow in interactome analyses of various species, also nonmodel organisms.[Abstract] [Full Text] [Related] [New Search]