The Relationship between Thermodynamic Stability and Molecular Structure of Lys25-Ribonuclease T₁

• Suzuki Rintaro

  Biotechnology Research Center, University of Tokyo

• Kojima Masaki

  Tokyo University of Pharmacy and Life Science

• Tanokura Masaru

  Biotechnology Research Center, University of Tokyo

抄録

RNase T₁ has two isozymes, Gln25- and Lys25-isoforms. The latter is relatively more stable than the former, although enzymatic activities are the same in both isozymes. Conformations of the two isoforms are not distinguished from each other crystallographically. To elucidate the mechanism of this phenomenon as based on the three-dimensional structure, energy minimization calculations with and without restraints were carried out for the complexes of guanosine 3'-monophosphate (3'-GMP) with Lys25-RNase T₁. The results indicated that the stability is mainly due to the electrostatic interaction of Lys25 with Asp29 and/or Glu31, not with Glu28 as reported previously.

収録刊行物

• bioimages

  bioimages 3 (2), 65-69, 1995

  日本バイオイメージング学会

キーワード

• Ribonuclease T₁
• Gln25-ribonuclease T₁
• Lys25-ribonuclease T₁
• conformation
• energy minimization
• torsion force

詳細情報

• CRID: 1390574876232627456
• NII論文ID: 10002037523
• NII書誌ID: AA11084187
• DOI: 10.11169/bioimages.3.65
• ISSN: 09192719
• 本文言語コード: en
• データソース種別:
  • JaLC
  • CiNii Articles
• 抄録ライセンスフラグ: 使用不可