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• W14611483 abstract "Collagen is the most abundant protein in the vertebrate body, and it is the major constituent of most connective tissues. The characteristic differences in the properties of tissues such as tendon, cartilage, artery, and skin are explained by the varying amounts of proteoglycans, glycoproteins, and elastin associated with the collagen. The physical strength of collagen fibers is a consequence of the molecular structure of the collagen fibril monomer, its packing arrangement in the collagen fibril, and the formation of covalent cross-links between the monomers in the fibrils. The collagen fibril monomer is essentially a stiff rod-like molecule composed of three polypeptides and a chain arranged in a triple-helical conformation. The presence of covalent disulphide linkages between the C-terminal peptides suggests that the extension peptides may play a role in the assembly process. The rate of helix formation varies among cell types, and, hence, the time available for the hydroxylases and glycosyltransferases to act on the non-helical substrate can vary. The higher levels of hylys and hylys-glycosides in cartilage collagen and lens capsule collagen as compared to tendon collagen can, therefore, be accounted for in part by the longer time required to achieve a helical conformation in chondrocytes and lens epithelial cells." @default.
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• W14611483 date "1979-01-01" @default.
• W14611483 modified "2023-09-26" @default.
• W14611483 title "THE SYNTHESIS AND PROCESSING OF COLLAGEN PRECURSORS" @default.
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• W14611483 doi "https://doi.org/10.1016/b978-0-08-023177-8.50008-1" @default.
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