English  |  正體中文  |  简体中文  |  Items with full text/Total items : 70548/70548 (100%)
Visitors : 23170864      Online Users : 311
RC Version 7.0 © Powered By DSPACE, MIT. Enhanced by NTU 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


    Please use this identifier to cite or link to this item: http://ir.lib.ncu.edu.tw/handle/987654321/27722


    Title: Thermostability of the N-Terminal RNA-Binding Domain of the SARS-CoV Nucleocapsid Protein: Experiments and Numerical Simulations
    Authors: Fang,HJ;Chen,YZ;Li,MS;Wu,MC;Chang,CL;Chang,CK;Hsu,YI;Huang,TH;Chen,HM;Tsong,TY;Hu,CK
    Contributors: 數據分析方法研究中心
    Keywords: ACUTE RESPIRATORY SYNDROME;CHEMICAL-SHIFTS;FORCE QUENCH;FINITE-SIZE;CORONAVIRUS;SEQUENCE;VIRUS;COOPERATIVITY;MECHANISM;PATHWAYS
    Date: 2009
    Issue Date: 2010-06-29 19:12:38 (UTC+8)
    Publisher: 中央大學
    Abstract: Differential scanning calorimetry, circular dichroism spectroscopy, nuclear magnetic resonance spectroscopy, and numerical simulations were used to study the thermostability of the N-terminal RNA-binding domain (RBD) of the SARSCoV nucleocapsid protein. The transition temperature of the RBD in a mixing buffer, composed of glycine, sodium acetate, and sodium phosphate with 100 mM sodium chloride, at pH 6.8, determined by differential scanning calorimetry and circular dichroism, is 48.74 degrees C. Experimental results showed that the thermal-induced unfolding-folding transition of the RBD follows a two-state model with a reversibility >90%. Using a simple Go-like model and Langevin dynamics we have shown that, in agreement with our experiments, the folding of the RBD is two-state. Theoretical estimates of thermodynamic quantities are in reasonable agreement with the experiments. Folding and thermal unfolding pathways of the RBD also were experimentally and numerically studied in detail. It was shown that the strand 01 from the N-terminal folds last and unfolds first, while the remaining beta-strands fold/unfold cooperatively.
    Relation: BIOPHYSICAL JOURNAL
    Appears in Collections:[數據分析方法研究中心 ] 期刊論文

    Files in This Item:

    File Description SizeFormat
    index.html0KbHTML644View/Open


    All items in NCUIR are protected by copyright, with all rights reserved.

    社群 sharing

    ::: Copyright National Central University. | 國立中央大學圖書館版權所有 | 收藏本站 | 設為首頁 | 最佳瀏覽畫面: 1024*768 | 建站日期:8-24-2009 :::
    DSpace Software Copyright © 2002-2004  MIT &  Hewlett-Packard  /   Enhanced by   NTU Library IR team Copyright ©   - Feedback  - 隱私權政策聲明