Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1987070 | International Journal of Biological Macromolecules | 2013 | 6 Pages |
Abstract
The structure of fibrous collagen, a long triple helix that self-associates in a staggered array to form a matrix of fibrils, fibers and fiber bundles, makes it uniquely suitable as a scaffold for biomaterial engineering. A major challenge for this application is to stabilize collagen structure by means that are acceptable for the end use. The bovine type I collagen microfibril model, built by computer assisted modeling, comprised of five right-handed triple helices in a left-handed super coil containing gap and overlap regions as well as the nonhelical telopeptides is a tool for predicting or visualizing chemistry to stabilize the matrix, insert an active agent, or otherwise modify collagen.
Keywords
Related Topics
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Biochemistry, Genetics and Molecular Biology
Biochemistry
Authors
Eleanor M. Brown,