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We carried out dynamic force manipulations $in$ $silico$ on a variety ofsuperhelical protein fragments from myosin, chemotaxis receptor, vimentin,fibrin, and phenylalanine zippers that vary in size and topology of their$\alpha$-helical packing. When stretched along the superhelical axis, allsuperhelices show elastic, plastic, and inelastic elongation regimes, andundergo a dynamic transition from the $\alpha$-helices to the $\beta$-sheets,which marks the onset of plastic deformation. Using Abeyaratne-Knowlesformulation of phase transitions, we developed a theory to model mechanical andkinetic properties of protein superhelices under mechanical non-equilibriumconditions and to map their energy landscapes. The theory was validated bycomparing the simulated and theoretical force-strain spectra. Scaling laws forthe elastic force and the force for $\alpha$-to-$\beta$ transition to plasticdeformation can be used to rationally design new materials of requiredmechanical strength with desired balance between stiffness and plasticity.

Dynamic transition from $\alpha$-helices to $\beta$-sheets in polypeptide superhelices