Figure 3. Force-dependent unbinding probabilities (top) and transition rates (bottom) and their best model fits (solid and dashed curves) reveal the energy and kinetics of C2 binding at zero force (Table 1).

Unbinding probabilities and rates are indicated by solid symbols, while binding rates are shown by hollow symbols.

Figure 3—figure supplement 1. Diagram illustrating the effect of membrane tethering on protein binding to the membrane.

The protein, shown here as the E-Syt2 C2AB, is tethered on the membrane at a point h₀ away from the membrane surface, via a flexible polypeptide linker with a contour length L. The other end of the linker is attached to the membrane-bound protein at a point h₁ away from the membrane.