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. 2013 Apr 15;27(8):928–940. doi: 10.1101/gad.216531.113

Figure 5.

Figure 5.

ITC-binding curves of complex formation between the QKI STAR protein and its RNA targets. (A) Sequence of 11-mer RNA (5′-UUCACUAACAA-3′) used for ITC titration studies in B–E. (B–E) ITC-binding curve complex formation of wild-type QKI STAR (B), the QKI STAR K190A/Q193A double mutant, (C) the QKI STAR N97A/R130A double mutant (D), and the QKI STAR K120A/R124A double mutant (E) with the 11-mer RNA target. Solid lines indicate nonlinear least-squares fit to the titration curve, with ΔH (binding enthalpy kcal mol−1), Ka (association constant), and N (number of binding sites per monomer) as variable parameters. Calculated values for Kd (dissociation constant) and N are indicated.