Large Flexibility of Dihydrofolate Reductase as Revealed by Temperature Effects on the Volume and Compressibility

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著者

    • OHMAE Eiji
    • Department of Chemistry, Faculty of Science, Hiroshima University
    • GEKKO Kunihiko
    • Department of Chemistry, Faculty of Science, Hiroshima University

抄録

The partial specific volume and adiabatic compressibility of dihydrofolate reductase (DHFR) from <I>Escherichia coli</I> remarkably increased as temperature was higher, corresponding to the conformational changes as revealed by spectroscopic measurements. These results demonstrate that this protein has a highly flexible structure at the native state whose tertiary structure or hydrophobic core is easily expanded with temperature to produce the internal cavities.

収録刊行物

  • Chemistry letters  

    Chemistry letters 1999(6), 507-508, 1999-06-05 

    The Chemical Society of Japan

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各種コード

  • NII論文ID(NAID)
    10004486273
  • NII書誌ID(NCID)
    AA00603318
  • 本文言語コード
    ENG
  • 資料種別
    ART
  • ISSN
    03667022
  • データ提供元
    CJP書誌  CJP引用  J-STAGE 
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