Table 2.

Results of chemical denaturation experiments for isolated I27, I28 modules and I27, I28 in I27-I28 dimer

Protein	[D]50%, M	ΔGD-N, kcal⋅mol−1	ku, s−1
I27 monomer	3.04  ± 0.01	7.6  ± 0.1	4.9 (±0.5)  × 10−4
I27 in dimer	3.24  ± 0.01	8.1  ± 0.1	6.0 (±3.0)  × 10−4
I28 monomer	0.93  ± 0.01	3.0  ± 0.1	1.6 (±0.3)  × 10−5
I28 in dimer	1.10  ± 0.02	3.5  ± 0.1	4.0 (±0.9)  × 10−6

[D]_50%, the concentration of denaturant at which 50% of the protein is denatured. ΔG_D-N, calculated thermodynamic stability. k_u, estimated unfolding rate at 0 M denaturant.