中大機構典藏-NCU Institutional Repository-提供博碩士論文、考古題、期刊論文、研究計畫等下載:Item 987654321/35604
English  |  正體中文  |  简体中文  |  Items with full text/Total items : 80990/80990 (100%)
Visitors : 40250633      Online Users : 256
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/987654321/35604


    Title: Compact dimension of denatured states of staphylococcal nuclease
    Authors: Chow,C. -Y.;Wu,Ming-Chya;Fang,Huey-Jen;Hu,Chin-Kun;Chen,Hueih-Min;Tsong,Tian-Yow
    Contributors: 數據分析方法研究中心
    Keywords: RESONANCE ENERGY-TRANSFER;LONG-RANGE STRUCTURE;RESIDUAL STRUCTURE;PROTEIN CONFORMATION;SPECTROSCOPIC RULER;FERRICYTOCHROME-C;ACID;KINETICS;FLUORESCENCE;STABILITY
    Date: 2008
    Issue Date: 2010-07-07 15:43:30 (UTC+8)
    Publisher: 中央大學
    Abstract: Fluorescence and circular dichroism stopped-flow have been widely used to determine the kinetics of protein folding including folding rates and possible folding pathways. Yet, these measurements are not able to provide spatial information of protein foldi
    Relation: PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
    Appears in Collections:[Research Center for adaptive Data analysis ] journal & Dissertation

    Files in This Item:

    File Description SizeFormat
    index.html0KbHTML582View/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 ©   - 隱私權政策聲明