Theoretical structure of the polar regions of the tropocollagen molecule
| Autor: | Alan G. Walton, A. J. Hopfingkr |
|---|---|
| Rok vydání: | 1970 |
| Předmět: |
chemistry.chemical_classification
Alanine Chemical Phenomena Tropocollagen Chemistry Stereochemistry Organic Chemistry Glycine Biophysics Peptide General Medicine Energy minimization Biochemistry Models Structural Biomaterials Crystallography Glutamates Models Chemical Helix Polar Molecule Collagen Polyproline helix |
| Zdroj: | Biopolymers. 9:433-444 |
| ISSN: | 1097-0282 0006-3525 |
| DOI: | 10.1002/bip.1970.360090406 |
| Popis: | 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 (27a and 27b). It is suggested that triple-strand structures of folded 27 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 α, polyproline II, and 27 helix structures. |
| Databáze: | OpenAIRE |
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