分子体積変化の追跡による蛋白質立体構造形成過程の解析 Volume Profile Analysis for Protein Folding

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抄録

By using spectroscopies under high pressure, we determined the volume changes associated with protein folding of reduced cytochrome c from the unfolded state to the native state. The pressure dependence of the equilibrium constant for the denaturation and the folding rate revealed that the volume change for the protein folding and the activation volume for the native state are negative. Such negative volumes can be accounted for by a decrease in volume resulting from the dehydration of hydrophobic groups, primarily the heme group, and the dehydration is mainly induced in the formation of the transition for the native state. We, therefore, propose that dehydration can compensate for the decreased entropy in the formation of protein structures, entropically promoting the protein folding reactions.

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 17(1), 13-22, 2007-05-20 

    The Japan Society of High Pressure Science and Technology

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各種コード

  • NII論文ID(NAID)
    10018918335
  • NII書誌ID(NCID)
    AN10452913
  • 本文言語コード
    JPN
  • 資料種別
    REV
  • ISSN
    0917639X
  • NDL 記事登録ID
    8742638
  • 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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