Destabilized protein domains are more extended and thus more susceptible to cleavage by a promiscuous protease, such as thermolysin or proteinase K (PK) . LiP involves brief treatment of lysate to protease followed by shotgun proteomics to characterize the yield of cleavage events . Loss of a tryptic peptide indicates a protein conformational change in the vicinity of that peptide sequence 107 . This peptide is modified at the C152 position with an adduct that corresponds to propachlor thiocarbamate. C156 is carbamidoylated by iodoacetamide. B) PRM chromatograms demonstrating the dependence of the adduct on propachlor treatment.