High-throughput profiling of protein/protein and drug/target interactions in human cells”. The abstract is below and the figure is attached

In my postdoctoral work, I focused on the cellular chaperone Hsp90 and how it recognizes its client proteins, using quantitative high-throughput protein/protein interaction assay LUMIER with BACON. We showed that Hsp90 client recognition is a combinatorial process: a cochaperone provides specificity at the protein fold level, whereas thermodynamic parameters determine the extent of client binding. Exploiting this finding, I further showed that chaperones can be used as thermodynamic sensors to characterize drug/target interactions in living cells and to identify novel targets for existing drugs. Finally, we have started to systematically characterize the chaperone/client interaction network using a combination of AP-MS and LUMIER.