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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 4. Thermodynamic analysis of CSL-KyoT2 binding interactions.

Figure 4

This figure shows representative thermograms (raw heat signal and nonlinear least squares fit to the integrated data) for KyoT2 binding to CSL. Forty titrations were performed per experiment, consisting of 7 μl injections that were spaced 120s apart. (A) Core CSL binding to KyoT2 residues 184-210. (B) Core CSL, pre-bound to a cognate DNA, binding to KyoT2 residues 184-210. (C) BTD binding to KyoT2 residues 184-210. (D) Core CSL binding to KyoT2 residues 182-210. (E) Core CSL binding to KyoT2 residues 182-196. (F) Thermodynamic profile of core CSL binding to KyoT2 residues 184-210. Thermodynamic parameters (ΔG°, ΔH°, and TΔS°) are plotted as a function of temperature (5, 15, 25, 35°C). The ΔCP of binding for the CSL-KyoT2 complex is −0.57 kcal/mol·K. See also Table S1 for buried surface at CSL-KyoT2 interface and Figure S3 for minimal KyoT2 peptide sequence that binds CSL.