Figure 2.

GdmCl-induced equilibrium unfolding transition of mutant α₁AT. Equilibrium unfolding of α₁AT was monitored by fluorescence spectroscopy with excitation at 280 nm and emission at 360 nm. Native α₁AT was diluted into an appropriate GdmCl solution and incubated at 25°C for 4 h. The buffer was 10 mM sodium phosphate/50 mM NaCl/1 mM EDTA, pH 6.5, and the final protein concentration was 5 μg/ml. ○, wild type; ●, G117A; ■, G117V; ▴, G117L; ▾, G117I; ♦, G117F.