Polyleucine α-helix coiled-coil interface
Molecular complementarity was discernable for all coiled-coil interfaces, with 20° rotation, for each of the polyleucine α-helical models (confirming knobs in holes interface). Local steric interactions resisted shear parallel to the helical axes and rotation normal to the helical axes; however, there was no discernable steric entanglement preventing translation normal to the helical axis. Even the lowest drop height evaluated (5 cm) resulted in complete unfolding (i.e., fractional folding = 0.0) (Fig. 5). The exceptions to this general characteristic were observed only for the antiparallel gauche+/gauche+ rotamer pair (dissociation midpoint of ~1 J/Kg), and the antiparallel trans/trans rotamer pair (dissociation midpoint of ~4 J/Kg).