  The macromechanical properties of purely bundled in vitro actin networks are
not only determined by the micromechanical properties of individual bundles but
also by molecular unbinding events of the actin binding protein (ABP) fascin.
Under high mechanical load the network elasticity depends on the forced
unbinding of individual ABPs in a rate dependent manner. Cross-linker unbinding
in combination with the structural self-similarity of the network enables the
introduction of a concentration/time superposition principle - broadening the
mechanically accessible frequency range over 8 orders of magnitude.
