Collagen model peptides: Sequence dependence of triple-helix stability
β Scribed by Anton V. Persikov; John A. M. Ramshaw; Barbara Brodsky
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 2000
- Tongue
- English
- Weight
- 470 KB
- Volume
- 55
- Category
- Article
- ISSN
- 0006-3525
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Collagen is a ubiquitous biomaterial that forms the supporting structures in skin, bone, tendons, cartilage, and blood vessels. Numerous types of collagen have been identified, and the tertiary structure of each shares the common structural motif of the collagen triple helix (CTH). [1] The CTH motif
## Synopsis Variations I-XVIII of a trimerlike cross-linked collagen model peptide were synthesized and used to investigate the cooperation of different neighboring Gly-X-Y tripeptides. The carboxyterminal decapentapeptide of the triple-helical part of collagen type I was chosen as the starting po
## Abstract This article deals with the effects of proline hydroxylation on collagen tripleβhelix stability, an issue that is still under discussion. To investigate the structural determinants of tripleβhelix stabilization by hydroxyproline (Hyp), we here characterized spectroscopically tripleβheli