The role of hydroxyproline in collagen folding: Conformational energy calculations on oligopeptides containing proline and hydroxyproline
✍ Scribed by M. Bansal; V. S. Ananthanarayanan
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1988
- Tongue
- English
- Weight
- 775 KB
- Volume
- 27
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
We have observed that the rate of folding of the enzymatically hydroxylated form of poly(G1y-Pro-Pro) into the triple-helical conformation is considerably higher than that of the unhydroxylated polypeptide [R. K. Chopra and V. S. Ananthanarayanan (1982) Proc. Nutl. Acud. Sci. USA 79, 7180-71841. In this study, we examine a plausible kinetic pathway for triple-helix formation by selecting peptide models for the unhydroxylated collagen molecule, and computing their conformational energies before and after proline hydroxylation. Starting with the available data on the preferred conformations of proline-and hydroxyproline-containing peptide sequences, energy minimization was carried out on the following pairs of peptides: