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    Please use this identifier to cite or link to this item: http://ir.lib.ncu.edu.tw/handle/987654321/33431


    Title: Microcalorimetrics studies of the thermodynamics and binding mechanism between L-tyrosinamide and aptamer
    Authors: Lin,Po-Hsun;Yen,Shih-Lun;Lin,Ming-Shen;Chang,Yung;Louis,Selva Roselin;Higuchi,Akon;Chen,Wen-Yih
    Contributors: 系統生物與生物資訊研究所
    Keywords: ISOTHERMAL TITRATION CALORIMETRY;RNA-PROTEIN RECOGNITION;IN-VITRO SELECTION;DNA APTAMERS;MOLECULAR RECOGNITION;INDUCED FIT;ARGININAMIDE COMPLEX;RIBOSWITCH;ENERGETICS;STABILITY
    Date: 2008
    Issue Date: 2010-07-07 11:30:37 (UTC+8)
    Publisher: 中央大學
    Abstract: In recent years, several high-resolution structures of aptamer complexes have shed light on the binding mode and recognition principles of aptamer complexe interactions. In some cases, however, the aptamer complex binding behavior and mechanism are not cl
    Relation: JOURNAL OF PHYSICAL CHEMISTRY B
    Appears in Collections:[Institute of Systems Biology and Bioinformatics] journal & Dissertation

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