Exploring a role in tanning for the gap region of the collagen fibril : catechin-collagen interactions / Eleanor M. Brown in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. CIII, N° 9 (09/2008)  

[article]  inJOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA) > Vol. CIII, N° 9 (09/2008) . - p. 290-297 Titre : Exploring a role in tanning for the gap region of the collagen fibril : catechin-collagen interactions Type de document : texte imprimé Auteurs : Eleanor M. Brown, Auteur ; Phoebe X. Qi, Auteur Année de publication : 2008 Article en page(s) : p. 290-297 Note générale : Bibliogr. Langues : Américain (ame) Index. décimale : 675.2 Préparation du cuir naturel. Tannage Résumé : Electron micrographs of stained collagen fibrils display a pattern of alternating light and dark bands perpendicular to the axis of the collagen fibril. Light bands correspond to regions of more dense lateral packing where adjacent collagen monomers overlap and dark bands correspond to 'gap' regions, domains of low-density molecular packing. Most studies of artificially stabilized collagen focus on crosslinks that utilize specific amino acid side chains, without considering whether these are more likely to be located in overlap or gap regions. The gap region with its lower molecular density, greater length, and available telopeptides appears promising as an area able to accommodate oligomeric compounds that are the typical tanning agents. This study uses the ERRC collagen microfibril model to explore the interactions of catechin, a model for vegetable tanning agents thought to interact with serine residues, in the collagen microfibril. Attempts at placing catechin near serine residues in the gap region of the microfibril and subjected to conditions typical of tanning. Under these simulated conditions each catechin molecule moved into a position where intermolecular stabilizing interactions were likely, although not with sering. The method will be valuable in predicting the effectiveness of proposed new tanning agents. En ligne : https://drive.google.com/file/d/1xP9BzPTM4FZdEKGyxqdWX2Lx_-aXij6Y/view?usp=drive [...] Format de la ressource électronique : Pdf Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=2511 [article]

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Molecular modeling of N-terminal telopeptides of bovine type I collagen / Phoebe X. Qi in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. XCVII, N° 6 (06/2002)  

[article]  inJOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA) > Vol. XCVII, N° 6 (06/2002) . - p. 235-243 Titre : Molecular modeling of N-terminal telopeptides of bovine type I collagen Type de document : texte imprimé Auteurs : Phoebe X. Qi, Auteur ; Eleanor M. Brown, Auteur Année de publication : 2002 Article en page(s) : p. 235-243 Note générale : Bibliogr. Langues : Américain (ame) Index. décimale : 675 Technologie du cuir et de la fourrure Résumé : Functionality, both biological and technological, follows from protein structure. Computer-assisted molecular modeling is a useful tool for visualizing structure-function relationships in proteins. A model of the triple helical portion of a bovine type I collagen microfbril was previously developed in our laboratory for use in studies of mechanisms of collagen crosslinking and modification. This model has now been enhanced by the addition of the N-terminal, nonhelical, telopeptides. The telopeptide region is highly flexible, allowing reactive side-chains of residues such as lysine to assume conformations favorable for interaction with adjacent triple helix chains. All naturally occurring collagen crosslinks are anchored in the telopeptide region. This enhancement to our model will enable us to visualize the effects of enzymatic crosslinking on collagen structure and stability. The current model is now more useful for studying mechanisms of inter- and intramicrofibril crosslinking of collagen by chemical and biochemical methods. The potential for transglutaminase crosslinking of collagen is explored with the model. En ligne : https://drive.google.com/file/d/1fyvNuAYfLxmLsoCIHZYmi-Oin2CYU_Oo/view?usp=drive [...] Format de la ressource électronique : Pdf Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=4292 [article]

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