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. 2004 May;13(5):1182–1196. doi: 10.1110/ps.03563704

Figure 6.

Figure 6.

Kinetics of disulfide-coupled folding of cp16 (A) and cp46 (B) BPTI. The fully reduced proteins were incubated in the presence of 80 mM DTTSS at pH 8.7, 25°C, and progress of the reactions was monitored by gel electrophoresis as described in the legends of Figs. 4 and 5. The filled symbols represent the relative intensities of the bands identified with the various species defined in Scheme 1: R (circles), I (squares), II (triangles), II′ (down triangles), and N (diamonds). The curves represent the values calculated by numerical integration of the kinetic scheme using the rate constants listed in Table 1.