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The triple helix is a specialized protein motif found in all collagens. Although X-ray diffraction studies of collagen began in the 1920s, the small amount of data available from fiber diffraction of collagen made the molecular structure determination difficult. In the early 1950s, two plausible fiber periods of about 20 and 30 Å were proposed, together with corresponding single-strand models having 7/2and 10/3-helical symmetry, respectively. The first framework of the triple helix was proposed by Ramachandran and Kartha in 1955. Rich and Crick proposed another structure with the same framework to avoid some of the steric problems of the first model. Their framework, which involved a triple-helical structure with a period of 28.6 Å and 10/3-helical symmetry, was the same as one of two single-strand models proposed at that time, except for the number of strands. On the other hand, Okuyama et al. detected the triple-strand model with the other framework, with a fiber period of 20 Å and 7/2-helical symmetry, in the single crystal of (Pro-Pro-Gly)10 in 1972. Although they proposed this structure as a new structural model for collagen, it has not been acknowledged as such, but instead has been regarded only as a model for a collagen-like peptide. Recently, we showed that both 7/2and 10/3-helical models could explain X-ray diffraction data from native collagen quantitatively. Furthermore, the helical symmetries of collagen-model peptides analyzed at high resolution are very close to the ideal 7/2-helical symmetry, whereas no supporting data was found for the 10/3-helical model. This evidence strongly suggests that an average molecular structure of native collagen is the 7/2-helical model rather than the prevailing Rich and Crick (10/3-helical) model.

The structure ofEpiphyas postvittanaTakeout 1 suggests a ligand-carrying role for Takeout proteins