New polypeptide conformations and their roles in molecular diseases of the vascular wall
| Autor: | L. W. Mitchell, M.M. Long, Dan W. Urry |
|---|---|
| Rok vydání: | 2009 |
| Předmět: |
chemistry.chemical_classification
biology Chemistry Stereochemistry Hydrogen bond Intermolecular force Supramolecular chemistry Polymer Condensed Matter Physics Atomic and Molecular Physics and Optics Hydrophobic effect medicine.anatomical_structure medicine biology.protein Physical and Theoretical Chemistry Elastin Protein secondary structure Elastic fiber |
| Zdroj: | International Journal of Quantum Chemistry. 10:107-118 |
| ISSN: | 1097-461X 0020-7608 |
| Popis: | New polypeptide conformations are described in which the repeating unit contains intrarepeat hydrogen bonding and in which there may or may not be hydrogen bonding between the repeating units. These conformations, called β spirals, were derived from polymers of repeat peptides of elastin, the connective tissue protein of the core of the elastic fiber. It is argued that these β spirals associate to form supramolecular fibrous constructs by intermolecular hydrophobic interactions and that these structures, which contain preferred though dynamic secondary structure, form elastomeric fibers which are not random. An appropriate understanding of these structures and their important biological properties require analysis from the disciplines of quantum chemistry, statistical mechanics, and the theory of rate processes. The manner in which these β-spirals associate, which is fundamental to the mechanism of fiber formation, provides insights into the molecular pathology of the vascular wall, specifically into the disruptive effects of decreased temperature, of lipid deposition, and of pathological calcification. |
| Databáze: | OpenAIRE |
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