  A self-consistent-field theory (SCFT) in the grand canonical ensemble
formulation is used to study transitions in a helix-coil multiblock copolymer
globule. The helices are modeled as stiff rods. In addition to the established
coil-globule transition we show for the first time that, even without explicit
rod-rod alignment interaction, the system undergoes a transition to a nematic
liquid-crystalline (LC) globular state. The LC-globule formation is driven by
the hydrophobic helical segment attraction and the anisotropy of the globule
surface energy. The full phase diagram of the copolymer was calculated. It
discriminates between an open chain, amorphous globule and LC-globule. This
model provides a relatively simple example of the interplay between secondary
and tertiary structures in homopolypeptides. Moreover, it gives a simple
explanation for the formation of helix bundles in certain globular proteins.
