The application of an in-cell proteome-wide structural biology method to identify drug-induced interactome changes

Abstract

Macromolecular crowding in the cell has an impact on protein interactions and binding affinities. This crowding effect may lead to differences in protein behavior in the cell compared to studies conducted in dilute solutions. Owing to this, it is necessary to perform structural studies in intact cells. In recent years, mass spectrometry (MS)-based methods have emerged for in-cell structural studies. These methods harness the power of the bottom-up proteomics workflow, where proteins are digested into peptides and analyzed by liquid chromatography coupled to mass spectrometry (LC-MS/MS).