The TRiC chaperonin is essential for folding and activating 10-15% of human proteins, and is required for cell survival. The complex consists of eight essential proteins, and small molecule inhibitors of the archaeal homolog Mm-CPN could be useful for studying chaperonin activity. An assay using the HTRF Transcreener ADP kit was developed in 1536-well plate format, based on the TR-FRET principle, to identify inhibitors of chaperonin activity. The assay measures ATP turnover resulting in a reduction of TR-FRET signal. Is the molecule effective to this assay?