Figure 2: Urea-induced equilibrium unfolding of UCH-L5N240. | Scientific Reports

Figure 2: Urea-induced equilibrium unfolding of UCH-L5N240.

From: Entropic stabilization of a deubiquitinase provides conformational plasticity and slow unfolding kinetics beneficial for functioning on the proteasome

Figure 2

(A) Intrinsic fluorescence spectra of UCH-L5N240 as a function of urea concentration, which are colour-ramped from red to purple from 0 to 7.2ā€‰M urea. (B) Global-fit of the urea-induced fluorescence change as a function of urea concentration at multiple wavelengths as indicated. (C) SVD analysis of the equilibrium unfolding data. The values of the first two SVD components are shown as a function of urea concentration and are coloured blue and red, respectively. Inset: The normalized contributions of the first four SVD components of which the first two account for more than 95% of the total signals. (D) Far-UV CD spectra of UCH-L5N240 as a function of urea concentration, which are presented in the same scheme as in (A). (E,F) Global-fit and SVD analyses of the far-UV CD data, presented in the same scheme as (B,C), respectively.

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