Table 2 Kinetic parameters of UCH-L5N240 derived from stopped-flow fluorescence measurements.

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

Ā 

k1

k2

k3

k4

(sāˆ’1)

0.14 ± 0.03

0.80 ± 0.14

10.3 ± 1.8

1120 ± 740

mf (kcal molāˆ’1 Māˆ’1)

āˆ’1.09 ± 0.07

āˆ’0.82 ± 0.06

āˆ’0.96 ± 0.06

āˆ’1.65 ± 0.22

(sāˆ’1)

(8.1 ± 7.6)e-9

(1.9 ± 1.1)e-6

(3.1 ± 1.2)e-4

(3.1 ± 1.6)e-2

mu (kcal molāˆ’1 Māˆ’1)

1.88 ± 0.12

1.41 ± 0.08

1.07 ± 0.05

0.81 ± 0.07

mkin (kcal molāˆ’1 Māˆ’1)

2.97 ± 0.14

2.23 ± 0.10

2.03 ± 0.08

1.73 ± 0.14

Ī”G (kcal molāˆ’1)

9.86 ± 0.57

7.66 ± 0.36

6.16 ± 0.25

6.21 ± 0.50

[D]50% (M)

3.33 ± 0.15

3.44 ± 0.13

3.04 ± 0.10

2.52 ± 0.18