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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Three-dimensional-energy minimized models for calf skin type 1 collagen triple helix and microfibril : 1. The triple helical models / James M. Chen in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. LXXXVI, N° 12 (12/1991)  

[article]  inJOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA) > Vol. LXXXVI, N° 12 (12/1991) . - p. 475-486 Titre : Three-dimensional-energy minimized models for calf skin type 1 collagen triple helix and microfibril : 1. The triple helical models Type de document : texte imprimé Auteurs : James M. Chen, Auteur ; Stephen H. Feairheller, Auteur ; Eleanor M. Brown, Auteur Année de publication : 1991 Article en page(s) : p. 475-486 Note générale : Bibliogr. Langues : Américain (ame) Index. décimale : 675 Technologie du cuir et de la fourrure Résumé : Molecular modeling methods were applied to the development of three dimensional structures of typ 1 collagen triple helices. The initial model was based on a triple helix of (Gly-Pro-Hyp). The amino acid sequences of the alpha 1 and 2 chains of calf skin Type 1 structure was nergy minimized to form all possible stabilizing interactions within the protein. Specific intraction sites which may contribute to the stability of the collagen molecule can be identified in the triple helical modls. The models may be used to target potential domains in collagen that contain sites for crosslinking reactions with chronium and other agents; determine what constraints on size, shape and molecular characteristics are likely to describe the optimum crosslinking agents; and suggest the application of which analytial and spectroscopic will give the most rigorous test of the computer models. En ligne : https://drive.google.com/file/d/18kTOW6lP6Lr1yGyAdYw8jURC0V0eAo3P/view?usp=drive [...] Format de la ressource électronique : Pdf Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=8333 [article]

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Three-dimensional-energy minimized models for calf skin type 1 collagen triple helix and microfibril : 2. The "smith" microfibril / James M. Chen in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. LXXXVI, N° 12 (12/1991)  

[article]  inJOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA) > Vol. LXXXVI, N° 12 (12/1991) . - p. 487-497 Titre : Three-dimensional-energy minimized models for calf skin type 1 collagen triple helix and microfibril : 2. The "smith" microfibril Type de document : texte imprimé Auteurs : James M. Chen, Auteur ; Stephen H. Feairheller, Auteur ; Eleanor M. Brown, Auteur Année de publication : 1991 Article en page(s) : p. 487-497 Note générale : Bibliogr. Langues : Américain (ame) Index. décimale : 675 Technologie du cuir et de la fourrure Résumé : Molecular modeling methods were applied to the development of a three dimnsional structure for a Type 1 collagen microfibril model. The model was based on the energy minimized "smith" microfibril model containing the consesus plypeptide sequence (Gly-Pro-Hyp). The amido acid sequences of the alpha 1 and 2 chains of calf skin Type 1 collagen were substituted into the "collagen-like" (Gly-Pro-Hyp) "smith" microfibril model. The model was then energy minimized using molecular mechanics and evaluated structurally using graphics. Specific interaction sites which may contribute to the stability of collagen packing can be identified in this model. Computer graphics was used to display the Type 1 "smith" microfibril model to determine specific domains containing sites which would facilitate the evaluation of potential crosslinking agents. The Type 1 model can be used to suggest domains in collagen that contain on size, shape and molecular characteristics are likely to describe the optimum crosslinking agents; and the application of which analytical and spectroscopic techniques to real systems will give the most rigorous test of the computer models. En ligne : https://drive.google.com/file/d/1fUzaWSfuzZE6aS7ddhruaqPVy2zZ2Ywy/view?usp=drive [...] Format de la ressource électronique : Pdf Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=8334 [article]

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