About the Book
Please note that the content of this book primarily consists of articles available from Wikipedia or other free sources online. Pages: 31. Chapters: Keratins, Collagen, Amyloid, Actin, Hydrolyzed collagen, Elastin, Coilin, Keratin 19, Keratin 8, Keratin 18, Keratin 5, Keratin 17, Keratin 10, Cytokeratin, Keratin 20, Keratin 14, Keratin 16, Keratin 7, Keratin 2A, Keratin 9, Keratin 13, Keratin 4, Keratin 15, Fibrillin, Reticular fiber, Catenin, ParM, Keratin 6A, Keratin 12, Elastic fiber, Extensin, Claudin, Osteolathyrism, Scleroprotein, Keratin 6C, Lamin, Anchoring fibrils, Keratin 6B, Beta-keratin, Actin remodeling, Keratin 3, Corneous, Tonofibril, Keratohyalin, Hair keratin, FACIT collagen, Influenza virus nucleoprotein, Sclerotin, Type I keratin, Type II keratin, Elaunin, Spongin, Fibrillogenesis, Protein aggregation, Type II hair keratin, Type I hair keratin, Keratin 21. Excerpt: Collagen is a group of naturally occurring proteins found in animals, especially in the flesh and connective tissues of mammals. It is the main component of connective tissue, and is the most abundant protein in mammals, making up about 25% to 35% of the whole-body protein content. Collagen, in the form of elongated fibrils, is mostly found in fibrous tissues such as tendon, ligament and skin, and is also abundant in cornea, cartilage, bone, blood vessels, the gut, and intervertebral disc. In muscle tissue, it serves as a major component of the endomysium. Collagen constitutes one to two percent of muscle tissue, and accounts for 6% of the weight of strong, tendinous muscles. Gelatin, which is used in food and industry, is collagen that has been irreversibly hydrolyzed. The molecular and packing structures of collagen have eluded scientists over decades of research. The first evidence that it possesses a regular structure at the molecular level was presented in the mid-1930s. Since that time, many prominent scholars, including Nobel laureates Crick, Pauling, Rich and Yonath, and oth...
