中大學術數位典藏-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 987654321/101429
English  |  正體中文  |  简体中文  |  Items with full text/Total items : 94201/94201 (100%)
Visitors : 81643522      Online Users : 6300
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: https://ir.lib.ncu.edu.tw/handle/987654321/101429


    Title: Revisiting the streptavidin-biotin binding by using an aptamer and displacement isothermal calorimetry titration
    Authors: 陳文逸;Kuo, Tai-Chih;Tsai, Ching-Wei;Lee, Peng-Chen;Chen, Wen-Yih
    Contributors: 工學院化學工程與材料工程學系
    Keywords: Affinity constant measurement;Aptamers, Nucleotide - metabolism;Binding;Biotin;Biotin - chemistry;Biotin - metabolism;Calorimetry;Calorimetry - methods;Constants;Entropy;ligand-displacement isothermal titration calorimetry;Ligands;Molecular interactions;Protein Binding;Streptavidin - chemistry;Streptavidin - metabolism;streptavidin-biotin binding;thermodynamic parameters;Thermodynamics;Titration;Titration calorimetry
    Date: 2015-01-01
    Issue Date: 2026-04-21 14:33:40 (UTC+8)
    Publisher: John Wiley and Sons Ltd;England: Blackwell Publishing Ltd
    Abstract: 摘要: The association constant of a well‐known streptavidin–biotin binding has only been inferred from separately measured kinetic parameters. In a single experiment, we obtained Ka 1 × 1012 M−1 by using a streptavidin–binding aptamer and ligand‐displacement isothermal titration calorimetry. This study explores the challenges of determining thermodynamic parameters and the derived equilibrium binding affinity of tight ligand–receptor binding. Copyright © 2015 John Wiley & Sons, Ltd. For the first time, the complete thermodynamic parameters of the well‐known streptavidin (SA)‐biotin binding are obtained by using the ligand‐receptor isothermal titration calorimetry (LDITC) approaches, where the novel use of aptamers as the ligand analogs is proposed. The estimated Ka (1.0 × 1012 M−1) is slightly smaller than that derived from the separated kinetic studies of SA‐biotin binding. The large favorable enthalpy and entropy cost were obtained. This study demonstrates that aptamer and LDITC is a powerful tool for studying molecular interactions.
    其他題名: J. Mol. Recognit
    出版者: England: Blackwell Publishing Ltd
    出版日期: 2015-03
    出處: Journal of molecular recognition, 2015-03, Vol.28 (3), p.125-128
    資源來源: Wiley Online Library - AutoHoldings Journals
    版權: Copyright © 2015 John Wiley & Sons, Ltd.
    識別號: ISSN: 0952-3499
    識別號: ISSN: 1099-1352
    識別號: EISSN: 1099-1352
    識別號: DOI: 10.1002/jmr.2366
    識別號: PMID: 25615849
    Appears in Collections:[Department of Chemical and Materials Engineering] journal & Dissertation

    Files in This Item:

    File Description SizeFormat
    index.html0KbHTML14View/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