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    National Tsing Hua University Institutional Repository > 理學院 > 化學系 > 期刊論文 >  Is glycine a surrogate for a D-amino acid in the collagen triple helix?

    Please use this identifier to cite or link to this item: http://nthur.lib.nthu.edu.tw/dspace/handle/987654321/56763

    Title: Is glycine a surrogate for a D-amino acid in the collagen triple helix?
    Authors: Horng, Jia-Cherng;Kotch, Frank W.;Raines, Ronald T.
    教師: 洪嘉呈
    Date: 2007
    Publisher: Cold Spring Harbor Laboratory Press
    Relation: Protein Science,Cold Spring Harbor Laboratory Press,Volume: 16,Issue: 2,Pages: 208-215,Published: FEB 2007
    Keywords: D-ALANINE
    Abstract: Collagen is the most abundant protein in animals. Every third residue in a collagen strand is a glycine with phi, psi = -70 degrees, 175 degrees. A recent computational study suggested that replacing these glycine residues with D-alanine or D-serine would stabilize the collagen triple helix. This hypothesis is of substantial importance, as the glycine residues in collagen constitute nearly 10% of the amino acid residues in humans. To test this hypothesis, we synthesized a series of collagen mimic peptides that contain one or more D-alanine or D-serine residues replacing the canonical glycine residues. Circular dichroism spectroscopy and thermal denaturation experiments indicated clearly that the substitution of glycine with D-alanine or D-serine greatly disfavors the formation of a triple helix. Host-guest studies also revealed that replacing a single glycine residue with D-alanine is more destabilizing than is its replacement with L-alanine, a substitution that results from a common mutation in patients with collagen-related diseases. These data indicate that the glycine residues in collagen are not a surrogate for a D-amino acid and support the notion that the main-chain torsion angles of a glycine residue in the native structure (especially, phi > 0 degrees) are critical determinants for its beneficial substitution with a D-amino acid in a protein.
    URI: http://www.cshlpress.com/
    Appears in Collections:[化學系] 期刊論文

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