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. 2019 Dec 17;8:e48491. doi: 10.7554/eLife.48491

Figure 2. Hsp70-induced swelling increases the conformational free energy of the system.

Conformational free-energy differences Δ⁢G of the Hsp70/rhodanese complexes with respect to the unbound substrate (n = 0) plotted as a function of the corresponding radius of gyration Rg. Each point represents one of the 64 possible binding configurations with color code indicating the number of bound chaperones. The black curve was obtained using the model in Sanchez (1979) (see Appendix 2). (inset) Distribution of Δ⁢Δ⁢G corresponding to the free-energy cost for binding an additional Hsp70 to a chaperone/substrate complex.

Figure 2—source data 1. Data from simulation results and Sanchez theory used to generate the plot in Figure 2 and the histogram in the inset of Figure 2.

Figure 2.

Figure 2—figure supplement 1. Free energy computation of different combinations of bound chaperones from steered MD simulations.

Figure 2—figure supplement 1.

Top: representative chaperone/rhodanese complex in the fully-stretched conformation. Bottom: Free-energy difference δ⁢G between equilibrium conformations and the fully-stretched state for rhodanese (red line) and two representative chaperone/rhodanese complexes. The double arrows indicate the final value of Δ⁢G for the corresponding complex.
Figure 2—figure supplement 1—source data 1. Simulation data used to generate the free energy plots; the work performed by the pulling force for each trajectory is also included in the subfolders.