This chapter discusses that the unique features of connective and skeletal tissues are their diversity and morphological character. Morphologically, connective tissue consists of fibrous proteins, ground substance, and cells. Before 1970, all vertebrate collagens were regarded as a simple class of molecules composed of two α1chains and one α2 chain, with only minor heterogeneity in composition between species. Collagen, a glycoprotein, is the longest of all protein molecules and is composed of tropocollagen monomers which are 300 nm long and 1.5 nm in diameter. The chapter discusses that twenty or twenty-one different amino acids are known to be present in different collagen types. The synthesis of a protein in living cells involves placing the amino acids in the proper sequence, determined by the genetic code, and linking them together by α peptide linkages. The macromolecular components of collagen are synthesized in large part at a ribosomal-messenger RNA complex within the cytoplasm of a family of mesenchymal cells, which include fibroblasts, chondroblasts, and osteoblasts. Proteins have no parallel in their structural and textural versatilities. The chapter discusses that although nature has designed proteins to perform specific roles in situ, they can display multifunctional properties by appropriate manipulations and processing treatments in different food systems. Animal skins contain the bulk deposit of collagen, thus, byproducts of the tannery can be utilized in the commercial production of edible fibrous collagen.
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