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. 2008 Jul 23;105(30):10360–10365. doi: 10.1073/pnas.0805326105

Fig. 3.

Fig. 3.

Effects of PhiKan083 on T-p53C-Y220C. (A) Changes in chemical shifts (normalized) vs. concentration for 15 resonances of T-p53C-Y220C in the presence of PhiKan083 at 20°C. The data are fitted to a single-site binding model. (B) Thermal denaturation of T-p53C-Y220C (10 μM) in the presence of PhiKan083. Denaturation is irreversible. However, at the very high heating rate of 270 K/h, the measured Tm is close to the reversible value. The data are fitted to the equation: T = Tm/(1 − (R/ΔS D-N(Tm))ln(1 + [L]/Kd)), where T is the observed melting temperature, Tm that in the absence of ligand L, Kd its dissociation constant, and ΔSD-N(Tm) the entropy of denaturation at Tm (the derivation is in the legend to Fig. S5). (C) Effect of PhiKan083 on kinetics of thermal denaturation at 37°C.