Figure 1.5.

(A) Hypothetical chevron plot of the apparent refolding and unfolding rates versus the final urea concentration. The continuous line represents a fit to a two-state kinetic folding model (Ferguson et al., 1999) with the following parameters: $k_f^{H_{2}O}=200{\sec }^{-1}$, $k_U^{H_{2}O}=0.015{\sec }^{-1}$, m_N-TS = 0.7, m_U-TS = 0.6, ΔG^H₂O = 5.62 kcal/mol, m-value = 1.3 kcal/mol/M, ${\text{urea}}_{\left\{\frac{1}{2}\right\}}=4.3M$. (B) Example of a sequential pathway with one on-pathway intermediate written in the text format for KINSIM. X1, X2, and X3 are the extinction coefficients of U, I, and N, respectively. (C) Hypothetical example of a refolding reaction of 10 μM protein for 10 s. The populations of species, shown by the continuous lines, are labeled as U, I, N, and U + I + N. The rates of the U to I and I to N transitions are 1 and 0.3 sec^-1, respectively. The values of X1, X2, and X3 are 0.01, 0.05, and 0.06, respectively.