Skip to main content
. Author manuscript; available in PMC: 2019 Apr 25.
Published in final edited form as: Chembiochem. 2014 Sep 15;15(16):2435–2442. doi: 10.1002/cbic.201402321

Figure 2.

Figure 2.

A) Schematic model of a two step inhibition mechanism. B) Time-dependent inhibition by DFTD. eEF-2K (100 nM) was incubated with different inhibitor concentrations (●, 500 μM; ▼, 250 μM; ▲, 125 μM; ◆, 62.5 μM; ■, 31.25 μM; and ◯, 0 μM) for different amounts of time (1, 5, 10, 20, 30, 60 and 120 min). The E+I mix was then diluted 50-fold into the assay reaction. The formation of the E•I* complex versus incubation time were fitted using KinTek Global Explorer for each inhibitor concentration. C) Reversibility of DFTD binding. eEF-2K (100 nM) was incubated with 250 μM inhibitor for 1 hour. The E+I mix was diluted 50-fold and incubated for several timepoints (0, 5, 10, 20, 30, 45, and 60 min) before starting the assay. Loss of the E•I* complex with time following dilution was fitted using KinTek Global Explorer.