Fig. 7.

Relationship of secondary and tertiary conformational features of the MD simulations. A. Fraction helicity for each residue averaged over the last 20% of the ensemble of eight AA S2-57 simulations. B. Schematic illustration of folding of discoidal double belt around hinges (open circles) to cover surface of sHDL. The pairwise helix 5 domain is green. C. Schematic illustration of folding of discoidal double belt and hairpin to cover surface of sHDL. The pairwise helix 5 domain and the helix 5 hairpin are green. The light blue arrow illustrates the dynamics of motion of the hairpin that swings in a right-handed spiral from the helix 5 pair to the N-terminal domains with an increase in simulation time (see supplementary Fig. III).