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    National Tsing Hua University Institutional Repository > 理學院 > 化學系 > 期刊論文 >  Characterization of the structure and dynamics of a near-native equilibrium intermediate in the unfolding pathway of an all beta-barrel protein

    Please use this identifier to cite or link to this item: http://nthur.lib.nthu.edu.tw/dspace/handle/987654321/56318

    Title: Characterization of the structure and dynamics of a near-native equilibrium intermediate in the unfolding pathway of an all beta-barrel protein
    Authors: Srimathi T;Kumar TKS;Chi YH;Chiu IM;Yu C
    教師: 余靖
    Date: 2002
    Publisher: American Society for Biochemistry and Molecular Biology
    Relation: JOURNAL OF BIOLOGICAL CHEMISTRY, American Society for Biochemistry and Molecular Biology, Volume 277, Issue 49, DEC 6 2002, Pages 47507-47516
    Abstract: The structure and dynamics of equilibrium intermediate in the unfolding pathway of the human acidic fibroblast growth factor (hFGF-1) are investigated using a variety of biophysical techniques including multidimensional NMR spectroscopy. Guanidinium hydrochloride (GdnHCl)-induced unfolding of hFGF-1 proceeds with the accumulation of a stable intermediate state. The transition from the intermediate state to the unfolded state(s) is cooperative without the accumulation of additional intermediate(s). The intermediate state induced maximally in 0.96 M GdnHCl is found to be obligatory in the folding/unfolding pathway of hFGF-1. Most of the native tertiary structure interactions are preserved in the intermediate state. H-1-N-15 chemical shift perturbation data suggest that the residues in the C-terminal segment including those located in the P-strands M X, and XI undergo the most discernible structural change(s) in the intermediate state in 0.96 M GdnHCl. hFGF-1 in the intermediate state (0.96 M GdnHCl) does not bind to its ligand, sucrose octasulfate. Limited proteolytic digestion experiments and hydrogen-deuterium exchange monitored by N-15 heteronuclear single quantum coherence (HSQC) spectra show that the conformational flexibility of the protein in the intermediate state is significantly higher than in the native conformation. N-15 spin relaxation experiments show that many residues located in beta-strands IX, X, and XI exhibit conformational motions in the micro- to millisecond time scale. Analysis of N-15 relaxation data in conjunction with the amide proton exchange kinetics suggests that residues in the beta-strands II, VIII, and XII possibly constitute the stability core of the protein in the near-native intermediate state.
    URI: http://www.asbmb.org/
    Appears in Collections:[化學系] 期刊論文

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