. 2014 Jun 10;22(6):889–898. doi: 10.1016/j.str.2014.03.014

Table 1.

Equilibrium Unfolding, Unfolding, and Refolding Kinetic Parameters

Variant	D_N-I (M)^a	m_N-I (kcal mol⁻¹ M⁻¹)^b	D_I-D (M)^c	m_I-D (kcal mol⁻¹ M⁻¹)^b	ΔG_N-I	ΔG_I-D	ΔG_N-D	k_U (min⁻¹)^e	k_fas (10⁻² s⁻¹)^f	k_slow (10⁻² s⁻¹)^f
Variant	D_N-I (M)^a	m_N-I (kcal mol⁻¹ M⁻¹)^b	D_I-D (M)^c	m_I-D (kcal mol⁻¹ M⁻¹)^b	(kcal mol⁻¹)^d			k_U (min⁻¹)^e	k_fas (10⁻² s⁻¹)^f	k_slow (10⁻² s⁻¹)^f
EGFP	2.04	2.55 ± 0.23	2.79	3.73 ± 0.27	5.18	10.37	15.55	2.09 ± 0.00	4.32 ± 0.08	1.00 ± 0.02
EGFP^G4Δ	1.76	1.96 ± 0.1	2.43	2.89 ± 0.14	3.46	7.01	10.47	2.15 ± 0.01	3.78 ± 0.25	1.15 ± 0.05

Concentration of GdmCl at which 50% of the protein sample is in the native and intermediate state.

Measure of dependence of ΔG on denaturant concentration, m value. Error bars represent 1 SD from three replicates.

Concentration of GdmCl at which 50% of the protein sample is in the intermediate and denatured state.

Change in free energy for native to intermediate (N-I), intermediate to denatured (I-D), and native to denatured (N-D) transitions.

Rate constant from single exponential fit of unfolding progress curves (data not shown). Error bars represent 1 SD from three replicates.

Rate constants from two exponential fits of refolding progress curves (Figure 2B). Error bars represent 1 SD from three replicates.