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    Please use this identifier to cite or link to this item: http://tkuir.lib.tku.edu.tw:8080/dspace/handle/987654321/117143


    Title: Intrinsic coordination for revealing local structural changes in protein folding-unfolding
    Authors: Shiu, Ying-Jen;Hayashi, Michitoshi;Shih, Orion;Su, Charlene;Tsai, Min-Yeh;Yeh, Yi-Qi;Su, Chun-Jen;Huang, Yu-Shan;Lin, Sheng-Hsien;Jeng, U-Ser
    Date: 2015-12-23
    Issue Date: 2019-09-26 12:11:03 (UTC+8)
    Publisher: Royal Society of Chemistry
    Abstract: With a deformed object of a rigid rod inside, the local dislocations may be tracked relatively easily with respect to the internal rigid rod. We apply this concept on protein folding-unfolding to track the internal structural changes of an unfolded protein in solution. Proposed here is a protein internal coordination based on the major axis X of an ellipsoidal protein and the stable intrinsic transition dipole moment μ of the protein during unfolding. In this methodology, small-angle X-ray scattering (SAXS) is used to provide the protein global morphologies in the native and unfolded states. Furthermore, time-resolved fluorescence anisotropy (TRFA) provides the relative orientation between X and μ of Trp59 of the model protein cytochrome c. Hence observed in the protein unfolding with denaturants, acid, urea, or GuHCl, is the elongation of the native protein conformation along a reoriented protein major axis; accompanied are the different extents of relocations of the terminal α helices and loop structures of the protein in the corresponding unfolding.
    Relation: Physical Chemistry Chemical Physics, 18(4), 3179
    DOI: 10.1039/c5cp06309d
    Appears in Collections:[Graduate Institute & Department of Chemistry] Journal Article

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