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. Author manuscript; available in PMC: 2015 Jan 7.
Published in final edited form as: Structure. 2013 Nov 27;22(1):70–81. doi: 10.1016/j.str.2013.10.010

Figure 5. Thermodynamic binding analysis of KyoT2 and CSL mutants.

Figure 5

This figure shows representative thermograms (raw heat signal and nonlinear least squares fit to the integrated data) for KyoT2 mutants KD196AA (A) and V186A (B) binding to wild-type core CSL; and CSL mutants F261R (C), V263E (D), A284R (E), and Q333R (F) binding to wild-type KyoT2 (184-210). Forty titrations were performed per experiment, consisting of 7 μl injections that were spaced 120s apart.