Accession Number : ADA185696

Title :   Synthesis of Two Component Models of Elastin,

Corporate Author : ALABAMA UNIV IN BIRMINGHAM LAB OF MOLECULAR BIOPHYSICS

Personal Author(s) : Prasad, Kari U ; Iqbal, M ; Urry, D W

PDF Url : ADA185696

Report Date : Jan 1986

Pagination or Media Count : 9

Abstract : Morphologically elastic fibers can be described as a fine fibrillar coating of a large amorphous core referred to as elastin. Elastin is an insoluble, highly cross linked and very hydrophobic protein with about 90% non polar amino acids and about 5% lysines. The insolubility of elastin is due to the presence of cross-links, primarily desmosine and isodesmosine, which are formed from four lysine residues, two each from two different peptide chains. The cross-linking sequences KAAAK and KAAK were observed to repeat at least six times in the soluble precursor protein, tropoelastin, which is comprised of 800-850 amino acids. Determination of the amino acid of porcine tropoelastin using tryptic peptides is 80% complete. A new mechanism of elasticity, a librational entropy mechanism, has been put forward to explain the elastic behavior of the polypentapeptide 2,3,4. The contrasts with the random chain network theory previously proposed for elastin.

Descriptors :   *AMINO ACIDS, *ELASTIC PROPERTIES, *FIBERS, ALBUMINOIDS, AMORPHOUS MATERIALS, BEHAVIOR, CHAINS, CORES, CROSSLINKING(CHEMISTRY), ENTROPY, HYDROPHOBIC PROPERTIES, MODELS, NETWORKS, PEPTIDES, PRECURSORS, PROTEINS, SEQUENCES, SOLUBILITY, SYNTHESIS, THEORY, SYNTHESIS(CHEMISTRY)

Subject Categories : Biochemistry

Distribution Statement : APPROVED FOR PUBLIC RELEASE