[article]
Titre : |
Model of the helical portion of a type I collagen microfibril |
Type de document : |
texte imprimé |
Auteurs : |
Eleanor M. Brown, Auteur ; Gregory King, Auteur ; James M. Chen, Auteur |
Année de publication : |
1997 |
Article en page(s) : |
p. 1-7 |
Note générale : |
Bibliogr. |
Langues : |
Américain (ame) |
Index. décimale : |
675 Technologie du cuir et de la fourrure |
Résumé : |
Collagen model - Collagens are an ubiquitous family of extracellular proetins in the animal world. Fibril-forming collagen in the animal world. Fibril-forming collagens are the major structural proteins. In addition to their biological function, collagens provide molecular frameworks that are utilized in the medical, food biological and technological, is a consequence of the basic structure of a protein. Computerized molecular modeling has been developed into a useful tool for visualizing structure-function relationships in proteins. The unique supramolecular characteristics of collagen have made it a suitable subject for model builders over more than thirty years. The bovine type I collagen microfibril model developed at ERRC now consists of 15 polypeptide chains of 315 amino acid residues each. This model is large enough to allow a comparison of its gross structurla features with the banding patterns obtained by electron microscopy. Measurable distances pertaining to the helix, triple helix, and microfibril are within experimetnal error of recently reported physical data on dried collagen samples. Two segments of the microfibril model, one rich in hydrophobic residues and the other rich in hydrophilic residues were examined in detail. The conformation of the hydrophobic segment more nearly matched the definitionb of collagen helix (57 %) than did the conformation of the hydrophilic segment (38 %). The model is potentially useful for studying mechanisms of both inter- and intra-microfibril crosslinking as well as for predicting the efficacy of specific modifications to the molecule or potential crosslinking agents. |
En ligne : |
https://drive.google.com/file/d/1x-LS4Y5scR6nNr71oaivn42_aARwpoD9/view?usp=drive [...] |
Format de la ressource électronique : |
Pdf |
Permalink : |
https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=9083 |
in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA) > Vol. XCII, N° 1 (01/1997) . - p. 1-7
[article]
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