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. 2005 Sep 19;102(39):13897–13902. doi: 10.1073/pnas.0505141102

Fig. 2.

Fig. 2.

Refolding kinetics of (HypCol13Cys2)3 at 25°C in the presence of 0.75 M GdmCl starting from equilibrium-unfolded protein. (A) Slow folding reaction [λ1 = 9.4 (±1.0) × 10–4 s–1] initiated by manual mixing. (B) Fast reaction measured in stopped-flow experiments. The kinetics are best described by a double-exponential function with rate constants of 19 ± 3 and 2.0 ± 0.6 s–1. The amplitudes of the two reactions cannot be compared directly because of different experimental setups required in the two experiments. The amplitudes of the fast reactions account for 20–30% of the total signal change.