Purchase includes free access to book updates online and a free trial membership in the publisher's book club where you can select from more than a million books without charge. Chapters: Cadherins, Igsf, Integrins, Selectins, Collagen, Fibronectin, Immunoglobulin Superfamily, Talin Protein, Laminin, Cd11a, L-Selectin, Mucin, P-Selectin, E-Selectin, Cell Adhesion Molecule, Carcinoembryonic Antigen, Lymphocyte Function-Associated Antigen 1. Excerpt: Collagen is a group of naturally occurring proteins. In nature, it is found exclusively in animals. It is the main protein of connective tissue. It is the most abundant protein in mammals, making up about 25% to 35% of the whole-body protein content. In muscle tissue it serves as a major component of endomysium. Collagen constitutes 1% to 2% of muscle tissue, and accounts for 6% of the weight of strong, tendinous muscles. Gelatin, which is used in food and industry, is derived from collagen. The molecular and packing structures of collagen have eluded scientists for decades; 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 (but not limited to) Nobel laureate Crick, Pauling, Rich, Yonath, Brodsky, Berman, and Ramachandran concentrated on the conformation of the collagen monomer. Several competing models although correctly dealing with the conformation of each individual peptide chain, gave way to the triple-helical "Madras" model which provided an essentially correct model of the molecule's quaternary structure although this model still required some refinement . The packing structure of collagen has not been defined to the same degree outside of the fibrillar collagen types, although it has been long known to be hexagonal or quasi-hexagonal . As with its monomeric structure, several conflicting models alleged that either the packing arrangement of collagen molecules is s... More: http://booksllc.net/?id=6058