The V30M Amyloidogenic Mutation Decreases the Rate of Refolding Kinetics of the Tetrameric Protein Transthyretin
Figure 1
(a) Example of a refolding kinetics experiment for WT-TTR monitored by the variation over time of the intrinsic fluorescence emission at 380 nm, pH 7.0, and 25°C. The curve (solid line) is the fit to the experimental data points using the simplest, best-fitting refolding model. The graph inset shows the spectral differences reflecting the conformational changes of TTR upon unfolding and refolding. (b) Schematic view of the TTR refolding mechanism.
