Research Article

Characterization of Flavonol Inhibition of DnaB Helicase: Real-Time Monitoring, Structural Modeling, and Proposed Mechanism

Figure 5

Inhibitory effects of flavonols on ssDNA binding of KpDnaB. EMSA of KpDnaB bound to dT30 (a) in the absence of any flavonol or presence of (b) Gal, (c) Kae, (d) Que, or (e) Myr. (f) The titration curves for ssDNA binding of KpDnaB. The apparent dissociation constant ( 𝐾 d , a p p ) values of KpDnaB bound to dT30 in the absence of any flavonol or presence of Myr, Que, Kae, or Gal, as determined from the titration curves, were 0.97 ± 0.07, 1.11 ± 0.05, 1.03 ± 0.07, 1.10 ± 0.05, and 1.03 ± 0.06 μM, respectively.
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