Figure 5.

The fly-casting speedup ratio, k_tot/k_Q=1, is plotted vs. the unfolded protein concentration assuming a binding stability corresponding to experiment. For K^bind = K^exp, fly casting speeds up binding 1.6 times the rate of the fully formed (Q_p = 1) protein through a range of reasonable protein concentrations. Parameters for the free energy functional are as in Fig. 2, and the contact radius is taken to be R₀ = 3 Å.