Figure 7: Thermal stabilization of p53 mutants by reactivation compounds. | Nature Communications

Figure 7: Thermal stabilization of p53 mutants by reactivation compounds.

From: Computational identification of a transiently open L1/S3 pocket for reactivation of mutant p53

Figure 7

Selected concentrations of PRIMA-1 (blue, square), MQ (green, circle) and stictic acid (red, triangle) were added to 4 μM of wild type, G245S and R175H core domain protein. Thermal stabilization was measured using DSF. Data points are plotted as the mean of sextuplet measurements, with corresponding 95% confidence intervals. Confidence interval bars not visible are smaller than the symbol used to plot the data point. PRIMA-1 and MQ stabilized each p53 variant about 1 °C or less over this range of concentrations. Stictic acid resulted in the greatest stabilization for both p53 mutants studied.

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