English  |  正體中文  |  简体中文  |  Items with full text/Total items : 54367/62174 (87%)
Visitors : 12775596      Online Users : 44
RC Version 6.0 © Powered By DSPACE, MIT. Enhanced by NTHU Library IR team.
Scope Tips:
  • please add "double quotation mark" for query phrases to get precise results
  • please goto advance search for comprehansive author search
  • Adv. Search
    HomeLoginUploadHelpAboutAdminister Goto mobile version
    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
    CRYSTAL-STRUCTURE
    ALPHA-HELIX
    BETA-TURNS
    PEPTIDES
    PROTEIN
    STABILITY
    DESIGN
    SIDE
    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/
    http://nthur.lib.nthu.edu.tw/dspace/handle/987654321/56763
    Appears in Collections:[化學系] 期刊論文

    Files in This Item:

    File Description SizeFormat
    index.html0KbHTML180View/Open


    在NTHUR中所有的資料項目都受到原著作權保護,僅提供學術研究及教育使用,敬請尊重著作權人之權益。若須利用於商業或營利,請先取得著作權人授權。
    若發現本網站收錄之內容有侵害著作權人權益之情事,請權利人通知本網站管理者(smluo@lib.nthu.edu.tw),管理者將立即採取移除該內容等補救措施。

    SFX Query

    與系統管理員聯絡

    DSpace Software Copyright © 2002-2004  MIT &  Hewlett-Packard  /   Enhanced by   NTU Library IR team Copyright ©   - Feedback