高圧NMRによる蛋白質研究の新しい展開-広い構造アンサンブルの探索- High Pressure NMR Enabling a Wide Conformational Search of Proteins

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著者

    • 赤坂 一之 AKASAKA Kazuyuki
    • 神戸大学大学院自然科学研究科分子集合科学専攻 Department of Molecular Science, Graduate School of Science and Technology, Kobe University

抄録

Many proteins are considered to perform their functions by dynamic excursion to "other" conformations that deviate from the basic structure found in crystal. These "other" conformations have seldom become targets of detailed structural study. The on-line cell high pressure NMR technique developed at Kobe is the only available technique capable of producing "other" conformations of proteins and simultaneously reporting their structures at residue-specific resolution using multi-dimensional NMR spectroscopy. The principle is based on the recognition that the partial molar volume of a protein strongly depends on its conformational state. Examples are given from two proteins, basic pancreatic trypsin inhibitor and the Ras-binding domain of RalGEF.

収録刊行物

  • 高圧力の科学と技術 = The Review of high pressure science and technology  

    高圧力の科学と技術 = The Review of high pressure science and technology 10(2), 88-94, 2000-05-20 

    The Japan Society of High Pressure Science and Technology

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各種コード

  • NII論文ID(NAID)
    10004668570
  • NII書誌ID(NCID)
    AN10452913
  • 本文言語コード
    JPN
  • 資料種別
    ART
  • ISSN
    0917639X
  • NDL 記事登録ID
    5358044
  • NDL 雑誌分類
    ZP1(科学技術--化学・化学工業)
  • NDL 請求記号
    Z17-1589
  • データ提供元
    CJP書誌  NDL  J-STAGE 
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