Table 3 Comparison of the folding kinetics of UCH-L1, -L3 and -L5N240.

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

Ā 

UCH-L1

UCH-L3

UCH-L5N240

(sāˆ’1)

0.3 ± 0.1

49 ± 20

0.14 ± 0.03

mf (kcal molāˆ’1 Māˆ’1)

āˆ’1.06 ± 0.10

āˆ’1.28 ± 0.10

āˆ’1.09 ± 0.07

(sāˆ’1)

(7.6 ± 2.3)e-5

(2.6 ± 0.9)e-4

(8.1 ± 7.6)e-9

mu (kcal molāˆ’1 Māˆ’1)

0.74 ± 0.04

0.83 ± 0.03

1.88 ± 0.12

mkin (kcal molāˆ’1 Māˆ’1)

1.80 ± 0.11

2.11 ± 0.10

2.97 ± 0.14

Ī”G (kcal molāˆ’1)

4.90 ± 0.27

7.19 ± 0.32

9.86 ± 0.57

[D]50% (M)

2.72 ± 0.13

3.41 ± 0.13

3.33 ± 0.15