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. 2021 Apr 26;12(21):7334–7349. doi: 10.1039/d1sc01739j

Fig. 1. Scheme of the protein constructs and amyloid-like characteristics of mutant p53C in vitro. (a) Scheme of the constructs used in the present study. P53C corresponds to the DNA-binding domain; P53 TAD-core corresponds to the transactivation domain (TAD) and the DNA-binding domain. P53 corresponds to the full-length version of p53. EGFP, enhanced green fluorescent protein. M237I and R249S correspond to the mutations in the Zn2+-binding site and DNA contact site, respectively. Domains are color-coded. (b) Line plot of fluorescence of thioflavin T (ThT) as a function of time for wt, M237I, and R249S p53C constructs. The data are shown as the mean ± s.e.m. of n = 3 independent experiments.

Fig. 1