Figure 2 | Scientific Reports

Figure 2

From: Cavity filling mutations at the thyroxine-binding site dramatically increase transthyretin stability and prevent its aggregation

Figure 2

Assessing Thermodynamic (A) and kinetic (B) stabilities of TTR mutants by urea unfolding. In (A), samples were incubated at 1.8 μM at different urea concentrations for 96 hours. Excitation was set to 280 nm while emission of fluorescence scanned from 300 to 400 nm. In (B) samples were incubated at 8 M urea and denaturation followed along time. The ratio in intensity between 355 and 335 nm was used to measure the extent of denaturation. Panel (C) shows the denaturation profile of the three variants probed by HHP. Samples were incubated at 1.8 μM and HHP increased. Also Trp fluorescence was used as a probe of denaturation.

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