Skip to main content
. Author manuscript; available in PMC: 2010 Mar 31.
Published in final edited form as: Biochemistry. 2009 Mar 31;48(12):2740–2751. doi: 10.1021/bi802327j

Table 1.

Observed rate constants for each step in the oxidative folding mechanism (eq. 1eq. 8) determined at pH 8.0, 25 °C

Redox-independent rate constants k’s (M−1 min−1)a k’s (M−1 min−1)b
k1 14.0 ± 0.14 18.0 ± 0.75
k2 2770 ± 51 2600 ± 357
k3 0.19 ± 0.01 0.20 ± 0.01
k4 14 ± 4.3 20 ± 5
k5 0.62 ± 0.01 0.63 ± 0.02
k6 45 ± 7.5 50 ± 7
k7 1.00 ± 0.07 1.0 ± 0.2
k8 1.28 ± 0.02 1.25 ± 0.07
k9 0.39 ± 0.03 0.41 ± 0.04
k10 0.59 ± 0.01 0.65 ± 0.04
k11 0.28 ± 0.01 0.22 ± 0.06
a)

computed from the original experimental data

b)

computed from the “experimental” data, created by varying the original k’s to test their uniqueness.