Transition state heterogeneity in GCN4 coiled coil folding studied by using multisite mutations and crosslinking -- Data Supplement - Supplemental Table 1 -- Proceedings of the National Academy of Sciences

Supplementary material for Moran et al. (1999) Proc. Natl. Acad. Sci. USA 96 (19), 10699-10704.

Table 2.
Parameters of dimeric GCN4-p2¢ folding

Species	Equilibrium		Kinetics
Species	-D G°	m °	R T ln k_f	R T ln k_u	- m_f	*m_u*	-D G° = D G^‡_u-DG^‡_f	m ° = m_u - m_f
Wild type	10.5 ± 0.1	1.8 ± 0.1	1.29 ± 0.05	-2.53 ± 0.12	0.93 ± 0.04	0.72 ± 0.03	10.2 ± 0.1	1.6 ± 0.1
D7G	8.7 ± 0.2	1.8 ± 0.1	1.10 ± 0.09	-1.24 ± 0.04	0.89 ± 0.08	0.72 ± 0.01	8.7 ± 0.1	1.5 ± 0.1
pD7A	9.4 ± 0.1	1.6 ± 0.1	1.16 ± 0.08	-2.4 ± 0.1	0.75 ± 0.07	0.71 ± 0.04	9.9 ± 0.2	1.5 ± 0.1
S14G	8.4 ± 0.1	1.6 ± 0.1	1.15 ± 0.12	-1.47 ± 0.04	0.90 ± 0.09	0.61 ± 0.01	9.0 ± 0.1	1.5 ± 0.1
S14A	10.6 ± 0.6	1.7 ± 0.2	1.43 ± 0.05	-3.15 ± 0.10	0.95 ± 0.03	0.78 ± 0.03	10.9 ± 0.1	1.7 ± 0.04
A24G	8.5 ± 0.2	2.0 ± 0.1	0.33 ± 0.11	-1.05 ± 0.05	0.60 ± 0.13	0.85 ± 0.016	7.8 ± 0.1	1.45 ± 0.13
AAA	11.3 ± .05	1.89 ± .02	1.70 ± 0.05	-2.54 ± 0.13	1.12 ± 0.03	0.69 ± 0.03	10.6 ± 0.1	1.8 ± 0.1
GGG	5.97 ± 0.02	1.95*	ND	-0.31 ± 0.18†	ND	0.86 ± 0.06†	ND	ND
TTT	9.00 ± 0.02	2.13 ± 0.01	0.54 ± 0.10	-2.03 ± 0.14	1.17 ± 0.12	0.87 ± 0.04	8.96 ± 0.17	2.04 ± 0.13
AAG	9.34 ± 0.01	1.99 ± 0.01	1.28 ± 0.08	-1.48 ± 0.06	0.95 ± 0.06	0.96 ± 0.02	9.2 ± 0.1	1.91 ± 0.06

All values extrapolated to zero denaturant concentration. The DG° values are referenced to 1 M standard state peptide concentration. Units of DG° and RT are kcal/mol. Units of m are kcal/mol per M.Observed second-order folding rates referenced to 5.5 mM peptide concentration. ND, not determined.

*Obtained from equilibrium denaturation measurement conducted in 5% 2,2,2-trifluroethanol.

^†Measured in 5% 2,2,2-trifluroethanol, which has been shown to have no effect on unfolding rates [Kentsis, A. & Sosnick, T. R. (1998) Biochemistry 37, 14613-14622].