Solvent molecules bridge the mechanical unfolding transition state of a protein

Dougan et al. 10.1073/pnas.0706075105.

Supporting Information

Files in this Data Supplement:

SI Text
SI Figure 6
SI Figure 7
SI Table 1

SI Figure 6

Fig. 6. Biphasic force dependence for unfolding of the I27 protein in glycerol solutions at different pulling velocities: The peak of the unfolding force distribution of the I27 protein as a function of concentration of glycerol, vol/vol, measured from force-extension unfolding at different pulling velocities. The mechanical stability of the I27 protein in aqueous glycerol solutions displays a biphasic force dependence for unfolding at a pulling speed of 400 nms^-1 (red squares) and 50 nms^-1 (black circles). The dashed line shows the expected force dependence at a pulling speed of 400 nms^-1 (red squares) and 50 nms^-1 (black circles).

SI Figure 7

Fig. 7. Force-clamp protein unfolding in aqueous solution and deuterium oxide aqueous solution. Multiple trace averages (n > 20 in each trace) of unfolding events measured using force-clamp spectroscopy for the I27 protein in; aqueous solution (light blue circles) for constant force measurements at 200 pN, 180 pN, 160 pN, 140 pN and 120 pN, and deuterium oxide (D₂O) aqueous solution (dark blue squares) at 200 pN, 180 pN, 160 pN, and 140 pN.

Table 1. Solvent bridging model with N interaction sites