Hydroimidazolone Modification of the Conserved Arg12 in Small Heat Shock Proteins: Studies on the Structure and Chaperone Function Using Mutant Mimics
Figure 7
Thermodynamic stability of wild type and mutant (R12A) αA-crystallin.
Equilibrium urea denaturation profile for 0.1 mg/ml wild type and mutant proteins at 25°C. The profile is normalized to a scale of 0 to 1. Symbols represent the experimental data points and the solid lines represent the best fit according to the three state model.