Scientific Reports

Table 1 Thermodynamic parameters of equilibrium unfolding of UCH-L1, -L3 and -L5_N240 induced by urea.

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

	UCH-L1^a	UCH-L3^b	UCH-L5_N240
	UCH-L1^a	UCH-L3^b	Fluorescence	Far-UV CD	Global fit
m (kcal mol⁻¹ M⁻¹)	2.95 ± 0.03	2.28 ± 0.06	2.73 ± 0.08	2.60 ± 0.04	2.61 ± 0.11
ΔG (kcal mol⁻¹)	8.83 ± 0.10	7.11 ± 0.20	9.56 ± 0.29	9.05 ± 0.15	9.21 ± 0.39
[D]_50% (M)	3.00 ± 0.003	3.12 ± 0.01	3.50 ± 0.01	3.48 ± 0.01	3.53 ± 0.01

^aThe values are taken from ref. 33 that correspond to the native-to-intermediate state transition and were derived from global fitting of fluorescence and far-UV CD data.
^bThe values are taken from ref. 27 derived from fluorescence data fitting to a two-state equilibrium model.

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