Model of the helical portion of a type I collagen microfibril / Eleanor M. Brown in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. XCII, N° 1 (01/1997)  

[article]  inJOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA) > Vol. XCII, N° 1 (01/1997) . - p. 1-7 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 [article]

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Use of computer-generated models in studies of modified collagen / Eleanor M. Brown in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. LXXXXI, N° 6 (06/1996)  

[article]  inJOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA) > Vol. LXXXXI, N° 6 (06/1996) . - p. 161-170 Titre : Use of computer-generated models in studies of modified collagen Type de document : texte imprimé Auteurs : Eleanor M. Brown, Auteur ; Gregory King, Auteur Année de publication : 1996 Article en page(s) : p. 161-170 Note générale : Bibliogr. Langues : Américain (ame) Catégories : Collagène Cuirs et peaux Molécules -- Modèles Simulation par ordinateur Index. décimale : 675 Technologie du cuir et de la fourrure Résumé : Production of leather from cattlehide is accomplished by the introduction of crosslinks between collagen triplehelices, microfibrils and fibrils. Present tanning technology uses chromium complexes to form crosslinks between acidic aminoacid side chains. Pretanning treatments that modify the primary amino groups of collagen have been reported to increase the efficiency of chrome tanning. To aide the effectiveness and efficiency of research leading to improved tanning technology, we have examined a fragment of our previously reported three dimensional model of the collagen microfibril.This 281 residue fragment of the microfibril model contains 15 lysine residues and 28 acidic residues distributed over the microfibril's 15 peptide chains. The effects of reductive alkylation and deamination of the lysine residues were simulated. Five independent binding sites in which carboxyl groups were located 7 to 11 Angström were indentified and a sphere of 8 Angström radius about the midpoint of each pair was isolated. The sites examined provide for the possibility of inter and intra microfibrillar stabilization. En ligne : https://drive.google.com/file/d/1tAZW6ISSgdVgJkto4EN_sILi8ZHq3sG0/view?usp=drive [...] Format de la ressource électronique : Pdf Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=7794 [article]

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