Table 1.

Thermodynamic parameters characterizing the unfolding transition of TMPKmt

	Fluorescence				Circular dichroism
Total dimer concentration	ΔG0.1a	m1b	ΔG0.2a	m2b	ΔG0.1a	m1b	ΔG0.2a	m2b
	Dimeric intermediate
10−7 M	6.06 ± 5.70	1.90 ± 1.83	13.55 ± 8.36	1.20 ± 1.44	ndc	nd	nd	nd
2.10−7 M	5.97 ± 14.97	1.74 ± 3.52	10.76 ± 14.37	0.51 ± 1.71	nd	nd	nd	nd
10−6 M	8.09 ± 1.93	2.34 ± 0.55	14.01 ± 4.01	1.42 ± 0.72	9.16 ± 2.71	2.66 ± 0.77	12.93 ± 3.05	1.23 ± 0.55
4.10−6 M	8.9 ± 2.4	2.3 ± 0.6	14.0 ± 6.9	1.4 ± 1.2	12.19 ± 9.34	3.12 ± 2.22	10.61 ± 6.10	0.91 ± 0.98
	Monomeric intermediate
10−7 M	16.23 ± 1.14	2.31 ± 0.39	5.51 ± 0.62	1.26 ± 0.06	nd	nd	nd	nd
2.10−7 M	18.16 ± 0.28	2.94 ± 0.05	6.43 ± 0.50	1.26 ± 0.12	nd	nd	nd	nd
10−6 M	18.55 ± 0.11	3.14 ± 0.04	6.21 ± 0.16	1.29 ± 0.02	18.47 ± 0.13	3.12 ± 0.02	6.12 ± 0.04	1.28 ± 0.02
4.10−6 M	18.26 ± 0.66	3.00 ± 0.18	6.10 ± 0.49	1.21 ± 0.05	18.72 ± 0.74	3.14 ± 0.22	6.14 ± 1.17	1.30 ± 0.15

The unfolding transitions at different protein concentrations were individually fitted to both equation 2 (dimeric intermediate) and equation 3 (monomeric intermediate) as developed in Materials and Methods. The errors correspond to standard deviations obtained from the fits.

^a In kCal • mole⁻¹.

^b In kCal • mole⁻¹ • M⁻¹.

^c nd, not determined.