Polypeptide alpha-carbon backbones were modeled as freely rotating cha
ins made up of spherical monomers. The monomers were assigned an abstr
act binary ''hydrophobicity'' property that could be either present or
absent. Under the assumption that ''hydrophobic'' residues tend to cl
uster together, away from the polar solvent, three-dimensional conform
ations of random copolymers of ''hydrophobic'' and ''hydrophilic'' mon
omers were calculated by a novel algorithm based on distance geometry
techniques. The simulated molecules were globular and compact in shape
, and possessed distinct hydrophobic cores, indicating that our method
was capable of reproducing some of the important global features of r
eal polypeptides. (C) 1994 John Wiley & Sons, Inc.