Equilibrium denaturation of WT and mutant pVHL.

Data are from normalized fluorescence emission at 337 nm after excitation in 295 nm. Data were collected in high salt buffer in the presence and absence of Arginine.Protein concentration was 5 µM.Tm- Melting temperature was calculated from intrinsic tryptophan fluorescence (337 nm) as a function temperature (4–80°C).[U]50%- Chemical denaturation by urea was calculated from intrinsic tryptophan fluorescence as a function Urea concentration (0–8 M) at 20°C.