Theoretical structure of the polar regions of the tropocollagen molecule

✍ Scribed by A. J. Hopfingkr; A. G. Walton

• Publisher: Wiley (John Wiley & Sons)
• Year: 1970
• Tongue: English
• Weight: 646 KB
• Volume: 9
• Category: Article
• ISSN: 0006-3525
• DOI: 10.1002/bip.1970.360090406

✦ Synopsis

The theoretical conformations of poly (Gly-Ala-Glu) have been studied. This peptide was chosen as a model for the glycine led triads of the polar regions in collagen. The most favorable conformations are found to be based on the extended and folded forms of the 27 helix ( 2 ~~ and 27b). It is suggested that triple-strand structures of folded Z7 helices exist in the polar collagen regions, and a structural model is presented which is in accord with recent ultrastructural deformation studies. It is a necessary condition for this structure that glycine occur in the lead of the peptide triads. In regions of the collagen molecule where the primary sequence does not contain triads (e.g., in the telopeptide region), random structures based on energy minimization of peptide neighbors are considered briefly. It seems likely that such regions contain an admixture of left-hand 01, polyproline 11, and 27 helix structures.