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[article]
Titre : |
Potential interactions of the C-terminal telopeptides of bovine type I collagen |
Type de document : |
texte imprimé |
Auteurs : |
Eleanor M. Brown, Auteur |
Année de publication : |
2004 |
Article en page(s) : |
p. 376-377 |
Note générale : |
Bibliogr. |
Langues : |
Américain (ame) |
Index. décimale : |
675 Technologie du cuir et de la fourrure |
Résumé : |
Type I collagen, the primary substrate for the tanning industry, is comprised of two al(I) and one a2(I) chains containing more than 3000 amino acid residues. More than 95% of each protein chain of the fibrillar collagenshas a repeating tripeptide sequence, Glycine-X-Y, where X and Y are often proline and hydroxyproline. This amino acid sequence imposes a rigid helical structure that coils into a triple helix and becomes the basis for supramolecular structures that give shape and integrity to organisms. The remaining 4% to 5% of the collagen molecule is composed of short extensions (telopeptides), without the tripeptide repeat, at the amino and carboxyl termini of the triple helix. These telopeptide regions, unlike the helical segments, are highly flexible, allowing reactive side-chains containing amine and carboxyl groups to assume conformations favorable for interactions with adjacent triple helix chains. Published reports of possible conformations for the carboxy terminal telopeptides of type I collagen were based on spectroscopic studies of the isolated peptides or on analysis of their amino acid sequences. The ERRC collagen microfibril model makes it possible to evaluate these predictions in the context of a supramolecular collagen structure. A conformation based on the collagen triple helix and a similar conformation predicted from NMR studies could be located within the gap region of the microfibril and would be suitable for interactions with neighboring triple helices. Conformations developed from solution studies of isolated peptides resulted in a telopeptide chain protruding out of the microfibril, and toward more distant helices. |
En ligne : |
https://drive.google.com/file/d/1KCNpWkXOxE_JKQY3JjKI32dBPrWELGc5/view?usp=drive [...] |
Format de la ressource électronique : |
Pdf |
Permalink : |
https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=4220 |
in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA) > Vol. XCIX, N° 9 (09/2004) . - p. 376-377
[article]
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