A Mass Spectrometry View of Stable and Transient Protein Interactions

摘要: Through an impressive range of dynamic interactions, proteins succeed to carry out the majority functions in a cell. These temporally and spatially regulated interactions provide means through which one single protein can perform diverse modulate different cellular pathways. Understanding identity nature these is therefore critical for defining their contribution health disease processes. Here, we overview workflows that incorporate immunoaffinity purifications quantitative mass spectrometry (frequently abbreviated as IP-MS or AP-MS) characterizing protein–protein interactions. We discuss experimental aspects should be considered when optimizing isolation complex. As presence nonspecific associations concern experiments, common sources present label-free metabolic labeling spectrometry-based methods help determine specificity The effective regulation pathways rapid reaction various environmental stresses rely on formation stable, transient, fast-exchanging While determining exact interaction remains challenging, review cross-linking approaches address this important aspect macromolecular assemblies.