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).