. 1999 Mar 2;96(5):1983–1988. doi: 10.1073/pnas.96.5.1983

Table 1.

Spectroscopic, stability, and kinetic properties of mutants

Mutants	Ellipticity 222 nm, mdeg	Fluorescence center of mass, nm	T_m, °C		ΔG_u, kcal/mol		Reduction in unfolding rate²	Increase in refolding rate³
Mutants	Ellipticity 222 nm, mdeg	Fluorescence center of mass, nm	Observed	Predicted¹	Observed	Predicted¹	Reduction in unfolding rate²	Increase in refolding rate³
3A	−73.1	336.5	57.7 ± 0.6	56.6 ± 1.1	–	10.9 ± 0.9	0.92	–
7A	−69.4	339.5	59.8 ± 0.6	54.9 ± 1.6	–	12.1 ± 1.3	2.9	–
11A	−70.5	338.2	69.2 ± 0.6	54.7 ± 2.0	–	7.3 ± 1.7	15.4	–
12A	−70.5	339.9	71.1 ± 0.6	59.8 ± 2.1	16.0 ± 0.5	7.3 ± 1.7	31.0	34.2
15A	−70.8	340.1	72.3 ± 0.6	59.1 ± 2.3	15.2 ± 0.5	7.2 ± 1.9	53.5	26.6
Arc-native	−69.4	336.7	57.9 ± 0.6	57.9 ± 0.6	11.0 ± 0.5	11.0 ± 0.5	1.0	1.0
Arc-denatured⁴		351.4

Calculated based on sum of ΔT_ms and ΔΔG_us for the single mutants (23).

Relative to wild-type Arc-st11 values in 4.6 M urea for 3A and 7A and in 4.5 M GuHCl for 11A, 12A, and 15A.

Relative to wild-type Arc-st11 value of 1.05⋅10⁷ M⁻¹⋅s⁻¹ (27).

⁴

Denatured in 6 M GuHCl.