By Karl. A. Piez (auth.), G. N. Ramachandran, A. H. Reddi (eds.)
Collagen is an engaging protein not just due to its ubiquitous incidence in multicellular animals, but in addition as a result of its distinctive chemi cal constitution. because the major constituent in bone, cartilage, epidermis, tendon, and the teeth, it isn't superb that collagen is of curiosity to anatomists, biochemists, biomedical engineers, mobilephone biologists, dermatolo gists, dental surgeons, leather-based chemists, orthopedic surgeons, physiologists, physicians, zoologists, and a number of others. This ebook was once deliberate to supply an updated entire survey of all elements of biochemistry of collagen. the new discovery of genetically specified collagens with tissue specificity has opened a brand new period in collagen biochemistry, and Karl Piez discusses this within the establishing bankruptcy on fundamental constitution. within the subsequent bankruptcy, Ramachandran and Rama krishnan take care of the molecular constitution of collagen, putting certain emphasis at the conformational facets of its polypeptide chains. stick with ing the honour of fundamental and secondary constitution of collagen, the 3-dimensional association of collagen molecules within the fibrils is roofed by way of Miller in bankruptcy three. Collagen is mostly within the insoluble country within the dwelling organism as a result cross-linking of person molecules, and Tanzer describes many of the facets of this cross-linkage in bankruptcy four. The biosynthesis of collagen is mentioned extensive by means of Prockop and his colleagues.
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Amino acid sequence of the N-terminal region of a2-CB4 from calf and rat skin collagen, FEBS Lett. 26:66. Fietzek, P. , Rexrodt, F. , Hopper, K. , 1973, The covalent structure of collagen. 2. The amino-acid sequence of al-CB7 from calf skin collagen, Eur. I Biochem. 38:396. Fietzek, P. , 1974a, Amino acid sequence of the aminoterminal region of calf skin collagen, Biochim. Biophys. Acta 365:305. Fietzek, P. , 1974b, Comparative sequence studies on a2CB2 from calf, human, rabbit, and pig-skin collagen, Eur.
F-! ,! f-! f - !. . , - - - - - - . . . . i .... ------'-.. ' ! ; , 023 9 4 103 5 o tive substitution). It it highly unlikely that this similarity could have arisen by chance. The two histidines are the only ones in the helical region, and hydroxylysine and phenylalanine are rare amino acids. It might be expected, therefore, that these regions have a critical function. It is possible, as explained below, that they are helical cross-link sites. It is known that the rodlike collagen molecules in the native fibril are staggered by multiples of 234 residues, a value referred to as D (Chapter 3), and that cross-links originate from lysine residues at positions 9 and 1044 in the nonhelical ends of the molecule.
1975, Conformational implications of amino acid sequence regularities in collagen, FEBS Lett. 15:94. , 1971, Evidence for a non-helical region at the carboxyl terminus of the collagen molecule, FEBS Lett. 13:101. , Miller, E. , 1972, Comparative electron microscope studies on the collagen extracted from cartilage, bone and skin, Eur. j. Biochem. 27: 192. , 1972, Non-helical regions in rat collagen al chain, FEBS Lett. 26:61. , and Nimni, M. , 1971, Properties of a collagen molecule containing three identical components extracted from bovine articular cartilage, Biochemistry 10:3905.