Table 5.

Rate constants of folding for five different positions in the iM structure found from fluorescence quenching

	tC°4	tC°9	tC°10	tC°12	tC°15
Fraction of pH 8 signal remaining after initial quenching	0.28 ± 0.01	0.36 ± 0.01	0.41 ± 0.01	0.31 ± 0.01	0.47 ± 0.02
Fast fluorescence rate constant (s−1)	1.150 ± 0.060	0.920 ± 0.060	1.460 ± 0.310	0.410 ± 0.070	0.412 ± 0.020
(A to B1/B2)
Fractional ΔF/Foa (A to B1/B2)	−0.07 ± 0.01	−0.07 ± 0.01	−0.06 ± 0.01	−0.04 ± 0.01	0.15 ± 0.01
Slow fluorescence rate constant (s−1)	0.018 ± 0.003	0.012 ± 0.004	0.038 ± 0.036	0.010 ± 0.001	0.012 ± 0.003
(B1/B2 to C)
Fractional ΔF/Foa (B1/B2 to C)	−0.01 ± 0.01	−0.01 ± 0.01	−0.02 ± 0.01	0.02 ± 0.01	−0.13 ± 0.01
Final fraction of pH 8 signal remaining after folding	0.20 ± 0.01	0.28 ± 0.01	0.33 ± 0.01	0.29 ± 0.01	0.49 ± 0.01

^aThe total ΔF/F_o signal amplitudes were normalized from 0.0 (initial) to 1.0 (final). Data were fit to the mechanism in Fig. 6.