The collagen triple-helix and the alpha-helical coiled coil represent the two basic supercoiled multi-stranded protein motifs. Originally they were characterized in fibrous proteins, but have been found more recently in a number of other proteins containing rod-shaped domains. Coiled-coil domains are responsible for the oligomerization of proteins, as well as other specific functions, while the triple-helix domains associate to form supramolecular structures and bind a variety of ligands. Both structures were originally solved by fiber diffraction, and recent crystallographic studies on small proteins and peptide models have confirmed the structure and provided molecular details. The differences in the molecular conformations of these two motifs and the interactions stabilizing these conformations are discussed. The molecular structures of both motifs constrain the amino acid sequence to recognizable patterns, requiring the (Gly-X-Y)(n) repeating sequence for the collagen triple-helix and a less stringent heptad repeat requirement (h-x-x-h-x-x-x)(n) for the coiled-coil domains, where h represents hydrophobic residues. The features and roles of these supercoiled domains in proteins are considered when they are found adjacent in the same protein.