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Molten-Globule of Proteins and Its Physiological Role

Research Project

Project/Area Number 02454536
Research Category

Grant-in-Aid for General Scientific Research (B)

Allocation TypeSingle-year Grants
Research Field 物質生物化学
Research InstitutionOsaka University

Principal Investigator

GOTO Yuji  Osaka Univ., Fac. of Sci., Associate Prof., 理学部, 助教授 (40153770)

Co-Investigator(Kenkyū-buntansha) TESHIMA Keizo  Hiroshima Univ., Fac. of Integrated Arts and Science, Associate Prof., 総合科学部, 助教授 (30155452)
Project Period (FY) 1990 – 1992
Project Status Completed (Fiscal Year 1992)
Budget Amount *help
¥7,000,000 (Direct Cost: ¥7,000,000)
Fiscal Year 1992: ¥700,000 (Direct Cost: ¥700,000)
Fiscal Year 1991: ¥700,000 (Direct Cost: ¥700,000)
Fiscal Year 1990: ¥5,600,000 (Direct Cost: ¥5,600,000)
Keywordsmolten globule / structure of proteins / protein denaturation / protein folding / cytochrome c / melittin / protein chemistry / small angle X-ray scattering / モルテン・グロビュ-ル構造 / チトクロムc / 合成ポリペプチド / 熱ショック蛋白質 / 静電相互作用 / チトクロムC / 合成ポリぺプチド
Research Abstract

The molten globule is a compact denatured state with a significant amount of secondary structure, but largely disordered tertiary structure. To understand the role of the molten globule in protein folding and its physiological role, we studied the conformation and stability of the molten globule of various proteins and the corresponding state of peptides. We obtained following major results.
1. The stability of the molten globule is determined by a balance of various forces. We showed that electrostatic repulsion is a critical factor destabilizing the molten globule state.
2. The molten globule of cytochrome c was studied by small angle X-ray scattering and its conformational properties were clarified.
3. We indicated that the reversibly denatured conformation of cytochrome c under physiological conditions (i.e. neutral ph, physiological temperature and no denaturant) is the molten globule.
4. We showed the mechanism of the anion and ph-dependent conformational transition of melittin and an amphiphilic polypeptide.
5. We showed that Guanidine-Hydrochloride induces the refolding of acid-unfolded proteins, stabilizing the molten globule state.

Report

(4 results)
  • 1992 Annual Research Report   Final Research Report Summary
  • 1991 Annual Research Report
  • 1990 Annual Research Report
  • Research Products

    (30 results)

All Other

All Publications (30 results)

  • [Publications] Goto,Y. & Aimoto,S.: "Anion and pH-dependent Conformational Transition of an Amphiphilic Polypeptide." J.Mol.Biol.218. 387-396 (1991)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1992 Final Research Report Summary
  • [Publications] Goto,Y. & Nishikiori,S.: "Role of Electrostatic Repulsion in the Acidic Molten Globule of Cytochrome C." J.Mol.Biol.222. 679-686 (1991)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1992 Final Research Report Summary
  • [Publications] Goto,Y. & Hagihara,Y.: "Mechanism of the Conformational Transition of Melittin" Biochemistry. 31. 733-738 (1992)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1992 Final Research Report Summary
  • [Publications] Hagihara,Y.,Kataoka,M.,Aimoto,S.& Goto,Y.: "Charge Repulsion in the Conformational Stability of Melittin" Biochemistry. 31. 11908-11914 (1992)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1992 Final Research Report Summary
  • [Publications] Kataoka,M.,Hagihara,Y.,Mihara.K. & Goto,Y.: "Molten Globule of Cytochrome c Studied by Small Angle X-Rya Scattering." J. Mol. Biol.229. 591-596 (1993)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1992 Final Research Report Summary
  • [Publications] Hagihara,Y.,Aimoto,S.Fink,A.L.& Goto,Y.: "Guanidine-Hydrochloride-Induced Folding of Proteins." J. Mol. Biol.

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1992 Final Research Report Summary
  • [Publications] Goto,Y., Takahashi,N. & Fink,A.L: "Mechanism of Acid-Induced Folding of Proteins." Biochemistry. 29. 3480-3488 (1990)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1992 Final Research Report Summary
  • [Publications] Goto, Y. & Fink, A.L: "Phase Diagram for Acidic Conformational States of Apomyoglobin." J. Mol. Biol.214. 803-805 (1990)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1992 Final Research Report Summary
  • [Publications] Goto, Y. & Aimoto, S: "Anion and ph-dependent Conformational Transition of an Amphiphilic Polypeptide." J. Mol. Biol. 218. 387-396 (1991)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1992 Final Research Report Summary
  • [Publications] Goto,Y., Okamura,N. & Aimoto, S: "ATP-induced Conformational Transition of Denatured Proteins." J. Biochem. 109. 746-750 (1991)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1992 Final Research Report Summary
  • [Publications] Goto, Y. & Nishikiori, S: "Role of Electrostatic Repulsion in the Acidic Molten Globule of Cytochrome c" J. Mol. Biol. 222. 679-686 (1991)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1992 Final Research Report Summary
  • [Publications] Goto, Y. & Hagihara, Y: "Mechanism of the Conformational Transition of Melittin." Biochemistry. 31. 733-738 (1992)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1992 Final Research Report Summary
  • [Publications] Hagihara,Y., Kataoka,M., Aimoto,S. & Goto,Y: "Charge Repulsion in the Conformational Stability of Melittin." Biochemistgry. 31. 11908-11914 (1992)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1992 Final Research Report Summary
  • [Publications] Kataoka,M.,Hagihara,Y., Mihara,K. & Goto,Y: "Molten Globule of Cytochrome c Studied by Small Angle X-Ray Scattering." J. Mol. Biol. 229. 591-596 (1993)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1992 Final Research Report Summary
  • [Publications] Hagihara,Y., Aimoto,S., Fink,A.L. & Goto,Y: "Guanidine-Hydrochloride-Induced Folding of Proteins." J. Mol. Biol.

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1992 Final Research Report Summary
  • [Publications] Yoshimura,T.,Goto,Y.& Aimoto,S.: "Fusion of Phospholipid Vesicles Induced by an Amphiphilic Model Peptide" Biochemistry. 31. 6119-6126 (1992)

    • Related Report
      1992 Annual Research Report
  • [Publications] Hagihara,Y.,Kataoka,M.,Aimoto,S. & Goto,Y.: "Charge Repulsion in the Conformational Stability of Melittin" Biochemistry. 31. 11908-11914 (1992)

    • Related Report
      1992 Annual Research Report
  • [Publications] Goto,Y.,Kogure,E.,Takagi,T.,Aimoto,S.& Aoba,T.: "Molecular Conformation of Porcine Amelogenin in Solution:Three Folding Units at the N-Terminal,Central,and C-Terminal Regions" J.Biochem.113. 55-60 (1993)

    • Related Report
      1992 Annual Research Report
  • [Publications] Kataoka,H.,Hagihara,Y.,Mihara,K. & Goto,Y.: "Molten Globule of Cytochrome c Studied by Small Angle X-Ray Scattering" J.Mol.Biol.229. 591-596 (1993)

    • Related Report
      1992 Annual Research Report
  • [Publications] Hagihara,Y.,Aimoto,S.,Fink,A.L. & Goto,Y.: "Guanidine-Hydrochloride-Induced Folding of Proteins" J.Mol.Biol.(1993)

    • Related Report
      1992 Annual Research Report
  • [Publications] 後藤 祐児: "蛋白質の立体構造形成反応 ー モルテン・グロビュール状態の構造と安定性 ー" 生化学. (1993)

    • Related Report
      1992 Annual Research Report
  • [Publications] Yuji Goto,N.Okamura & S.Aimoto: "ATP‐Induced Conformational Transition of Denatured Proteins." J.Biochem.109. 746-750 (1911)

    • Related Report
      1991 Annual Research Report
  • [Publications] Yuji Goto & S.Aimoto: "Anion and pH‐dependent Conformational Transition of an Amphiphilic Polypeptide." J.Mol.Biol.218. 387-396 (1991)

    • Related Report
      1991 Annual Research Report
  • [Publications] Yuji Goto & S.Nishikiori: "Role of Electrostatic Repulsion in the Acidic Molten Globule of Cytochrome c." J.Mol.Biol.222. 679-686 (1991)

    • Related Report
      1991 Annual Research Report
  • [Publications] Yuji Goto & Y.Hagihara: "Mechanism of the Conformational Transition of Melittin." Biochemistry. 31. 732-738 (1992)

    • Related Report
      1991 Annual Research Report
  • [Publications] 後藤 祐児: "球状蛋白質のモルテングロビュ-ル状態ー陰イオンによる安定化とその機構ー" 生物物理. 31. 122-128 (1991)

    • Related Report
      1991 Annual Research Report
  • [Publications] 後藤 祐児,高木 俊夫: "誌上対談 モルテン・グロビュ-ルをめぐって" 蛋白質核酸酵素. 37. 772-780 (1992)

    • Related Report
      1991 Annual Research Report
  • [Publications] Yuji Goto et al.: "Mechanism of AcidーInduced Folding of proteins." Bichemistry. 29. 3480-3488 (1990)

    • Related Report
      1990 Annual Research Report
  • [Publications] Yuji Goto & A.L.Fink: "Phase Diagram for Acidic Conformational States of Apomyoglobin." J.Mol.Biol.214. 803-805 (1990)

    • Related Report
      1990 Annual Research Report
  • [Publications] Yuji Goto & S.Aimoto: "Anionーand pHーdependent Conformational Transition of an Amphiphilic Polypeptide" J.Mol.Biol.

    • Related Report
      1990 Annual Research Report

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Published: 1990-04-01   Modified: 2016-04-21  

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