An aggregating elastin-like pentapeptide
| Autor: | M.A. Castiglione Morelli, A. DeStradis, M. DeBiasi, Antonio Mario Tamburro |
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| Rok vydání: | 1993 |
| Předmět: |
Magnetic Resonance Spectroscopy
Protein Conformation Molecular Sequence Data Supramolecular chemistry Concentration effect macromolecular substances Fibril Pentapeptide repeat law.invention Structural Biology law Amino Acid Sequence Agrégation Molecular Biology Aqueous solution biology Chemistry Circular Dichroism General Medicine Elastin Crystallography Microscopy Electron biology.protein Electron microscope Oligopeptides |
| Zdroj: | Journal of biomolecular structuredynamics. 11(1) |
| ISSN: | 0739-1102 |
| Popis: | Synthetic VGGVG, a “monomelic” unit of the glycine-rich regions of elastin, has been investigated for its molecular and supramolecular properties. In aqueous solution the pentapeptide showed conformational features strongly concentration-dependent. CD and NMR studies suggested a partial unfolding on increasing the concentration. Electron microscopy, on the other hand, evidenced extensive aggregation of the pentapeptide yielding elastin-like supramolecular structures constituted either by twisted ropes or by banded fibrils. |
| Databáze: | OpenAIRE |
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