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    National Tsing Hua University Institutional Repository > 理學院 > 化學系 > 期刊論文 >  2,2,2-Trifluoroethanol induces helical conformation in an all beta-sheet protein


    Please use this identifier to cite or link to this item: http://nthur.lib.nthu.edu.tw/dspace/handle/987654321/56383


    Title: 2,2,2-Trifluoroethanol induces helical conformation in an all beta-sheet protein
    Authors: Jayaraman, G;Kumar, TKS;Arunkumar, AI;Yu, C
    教師: 余靖
    Date: 1996
    Publisher: Elsevier
    Relation: BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, Elsevier, Volume 222, Issue 1, MAY 6 1996, Pages 33-37
    Keywords: SECONDARY STRUCTURES
    PEPTIDE
    TRIFLUOROETHANOL
    Abstract: The effect of 2,2,2-trifluoroethanol (TFE) on the structure of an all beta-sheet protein, cardiotoxin analogue II (CTX II), from the Taiwan cobra (Naja naja arm) is studied. Using circular dichroism studies, it is found that higher concentrations of TFE induced a structural transition from beta-sheet to alpha-helix, both in the native state (nCTX II) and in denatured but not disulfide reduced CTX II (dCTX II) samples. The beta-sheet to alpha-helix conversion is shown to be cooperative. However, in denatured and reduced CTX II (rCTX II), TFE transforms a portion(s) of the protein backbone from a random coil to an alpha-helical conformation. Based on the solution structure of CTX II and the physical property of TFE, a possible mechanism for the observed backbone structural transitions induced by TFE is discussed. The results described in this paper question the significance of the structure of the ''molten globule'' intermediate(s) obtained in organic solvents such as TFE.
    URI: http://www.elsevier.com/
    http://nthur.lib.nthu.edu.tw/dspace/handle/987654321/56383
    Appears in Collections:[化學系] 期刊論文

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