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. Author manuscript; available in PMC: 2012 May 24.
Published in final edited form as: Biochemistry. 2011 Apr 28;50(20):4350–4359. doi: 10.1021/bi200232c

Figure 1.

Figure 1

Titration with a tight-binding pyrrolidine inhibitor to determine the concentration of active AlkA. Experiments were performed using 1 µM 19mer I•T substrate (19u) with varying concentrations (from 0 to 400 nM) of 25mer pyrrolidine inhibitor (Y•T). The concentration of AlkA was 100 nM (●) and 200 nM (○). The fraction of active AlkA was determined by measuring the initial rate of product formation and plotting the relative rate (Vobs/Vmax) versus the concentration of inhibitor. The average and standard deviation of two to four replicates are shown. This titration gives an average value of 0.57 ± 0.03 for the fraction of active AlkA, assuming a single monomer binds to each DNA (11).