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1996 Fiscal Year Final Research Report Summary

Joint Study on the Mechanism of Protein Folding

Research Project

Project/Area Number 07044200
Research Category

Grant-in-Aid for international Scientific Research

Allocation TypeSingle-year Grants
SectionJoint Research
Research InstitutionOsaka University

Principal Investigator

GOTO Yuji  Osaka University, 大学院・理学研究科, 助教授 (40153770)

Co-Investigator(Kenkyū-buntansha) SEGAWA Shin-ichi  Kwansei Gakuin University, 理学部, 教授 (70103132)
KUWAJIMA Kunihiro  University of Tokoy, 大学院・理学系, 助教授 (70091444)
KAWATA Yasushi  Tottori University, 工学部, 助教授 (40177697)
KATAOKA Mikio  Osaka University, 大学院・理学研究科, 助教授 (30150254)
CHAN Hue Sun  University of California, San Francisco, 薬学部, 助教授
FINK A.L.  カリフォルニア大学, 化学生化学部, 教授
DOBSON C.M.  オックスフォード大学, 化学部, 教授
DILL Ken A  University of California, San Francisco, 薬学部, 教授
KIM P.S.  マサチューセッツ工科大学, 生物部, 教授
DOBSON Chris M  University of Oxford
FINK Anthony L  University of California, Santa Cruz
KIM Peter S  Massachusetts Institute of Technology
Project Period (FY) 1995 – 1996
KeywordsProtein / Denaturation / Protein folding / X-ray solution scattering / Molecular chaperone / Molten globule / Circular dichroism / beta-Lactoglobulin
Research Abstract

Elucidation of the mechanisms of protein folding, by which the genetic information contained in the primary amino acid sequence of a protein is transmitted to its unique three-dimensional structure, is essential for understanding the structure and function of proteins. We carried out the International Scientific Research Program in order to clarify various problems of protein folding and obtained the following results.
1. We characterized the conformation and stability of the molten globule and related states of various proteins including cytochrome c, apomyoglobin, and alpha-lactalbumin. In particular, we used solution X-ray scattering to characterize their compactness and shape. Based on the structural properties obtained by solution X-ray scattering, general and conceptual structural images for the molten globule states are described and compared with the model obtained by nuclear magnetic resonance. The results indicate that the term "molten globule" is used to describe a wide range … More of non-native conformations, none of them completely consistent with the original definition.
2. beta-Lactoglobulin, a predominantly beta-sheet protein, is an interesting example representing inconsistency of the local and non-local secondary structure preference. We have studied the folding kinetics of beta-lactoglobulin and showed that a partly alpha-helical intermediate accumulates transiently before formation of the native beta-sheet. The results suggest that the folding of beta-lactoglobulin follows a non-hierarchical mechanism, in which non-native alpha-helical structures play important roles. The similar alpha-helical intermediate was also detected during the equilibrium unfolding transition induced by Gdn-HCl.
3. To understand the conformational features required for the substrate of GroEL,a molecular chaperone, we studied the interactions of GroEL with various conformational states of horse cytochrome c. The results indicate that the fluctuating and exposed hydrophobic clusters of the substrates are responsible for the interaction, and that the interaction is modulated by electrostatic interaction. These characteristics are similar to those of the interaction of cychrome c derivatives with negatively charged phospholipid membranes, suggesting a common mechanism. Less

  • Research Products

    (36 results)

All Other

All Publications (36 results)

  • [Publications] Kataoka,Mikio: "X-ray solution scattering studies of protein folding" Folding & Design. 1. R107-R114 (1996)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] Kataoka,Mikio: "Structural characterization of molten globule of α-lactalbumin by solution X-ray scattering" Protein Sci.6. 422-430 (1997)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] Hoshino,Masaru: "Interaction of GroEL with conformational state of horse cytochrome c" J.Mol.Biol.262. 575-587 (1996)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] Hirota,Nami: "Cooperative α-helix formation of β-lactoglobulin and melittin induced by hexafluoroisopropanol" Protein Sci.6. 416-421 (1997)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] Hamada,Daizo: "Non-native α-helical intermediate in the refolding of β-lactoglobulin,a predominantly β-sheet protein" Nature Struct.Biol.3. 868-873 (1996)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] Semisotnov,G.V.: "Protein globularization during folding. A study by synchrotron small-angle X-ray scattering" J.Mol.Biol.262. 559-574 (1996)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] Hamada,Daizo: "Role of heme axial ligands in the conformational stability of the native and molten globule states of horse cytochrome c." J.Mol.Biol.256. 172-186 (1996)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] Hamada,Daizo: "High helical propensity of the peptide fragments derived from beta-lactoglobulin,a predominantly beta-sheet protein." J.Mol.Biol.254. 737-746 (1995)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] Nishii,ichiro: "Thermodynamic stability of the molten globule states of apomyoglobin" J.Mol.Biol.250. 223-238 (1995)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] Shiraki,Kentaro: "Trifluoroethanol-iduced stabilization of the alpha-helical structure of beta-lactoglobulin." J.Mol.Biol.245. 180-194 (1995)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] Kataoka,Mikio: "Structural characterization of the molten globule and native states of apomyoglobin by solution X-ray scattering." J.Mol.Biol.249. 215-228 (1995)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] Kawata,Yasushi: "The role of ATP hydrolysis in the function of the chaperonin GroEL-Dynamic complex formation with GroES." FEBS Letters. 369. 283-286 (1995)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] Kawajima,Kunihiro: "The molten globule state of alpha-lactalbumin." FASEB J.10. 102-109 (1996)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] Peng,Zheng-yu: "Local structural preferences in the alpha-lactalbumin molten globule." Biochemistry. 34. 3248-3252 (1995)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] Dill,Ken A.: "Principles of protein folding-A perspective from simple exact models." Protein Science. 4. 561-602 (1995)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] Balbach,Jochen: "Following protein folding in real time using NMR spectroscopy." Nature Struc.Biol.2. 865-870 (1995)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] Shi,Lee: "Conformational characterization of DnaK and its complexes with substrate protein by small-angle X-ray scattering." Biochemistry. 35. 3297-3308 (1996)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] Hamada,Daizo: "Salt-induced formation of the molten globule state of apomyoglobin studied by isothermal titration calorimetry." Thermochimica Acta. 266. 385-400 (1995)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] Kataoka, Mikio: "X-ray solution scattering studies of protein folding" Folding & Design. 1. R107-R114 (1996)

    • Description
      「研究成果報告書概要(欧文)」より
  • [Publications] Kataoka, Mikio: "Structural characterization of molten globule of alpha-lactalbumin by solution X-ray scattering" Protein Sci.6. 422-430 (1997)

    • Description
      「研究成果報告書概要(欧文)」より
  • [Publications] Hoshino, Masaru: "Interaction of GroEL with conformational state of horse cytochrome c" J.Mol.Biol. 262. 575-587 (1996)

    • Description
      「研究成果報告書概要(欧文)」より
  • [Publications] Hirota, Nami: "Cooperative alpha-helix formation of beta-lactoglobulin and melittin induced by hexafluoroisopropanol" Protein Sci.6. 416-421 (1997)

    • Description
      「研究成果報告書概要(欧文)」より
  • [Publications] Hamada, Daizo: "Non-native alpha-helical intermediate in the refolding of beta-lactoglobulin, a predominantly beta-sheet protein" Nature Struct.Biol.3. 868-873 (1996)

    • Description
      「研究成果報告書概要(欧文)」より
  • [Publications] Semisotnov, G.V.: "Protein globularization during folding. A study by synchrotron small-angle X-ray scattering" J.Mol.Biol.262. 559-574 (1996)

    • Description
      「研究成果報告書概要(欧文)」より
  • [Publications] Hamada, Daizo: "Role of heme axial ligands in the conformational stability of the native and molten globule states of horse cytochrome c" J.Mol.Biol.256. 172-186 (1996)

    • Description
      「研究成果報告書概要(欧文)」より
  • [Publications] Hamada, Daizo: "High helical propensity of the peptide fragments derived from beta-lactoglobulin, a predominantly beta-sheet protein" J.Mol.Biol.254. 737-746 (1995)

    • Description
      「研究成果報告書概要(欧文)」より
  • [Publications] Nishii, Ichiro: "Thermodynamic stability of the molten globule states of apomyoglobin" J.Mol.Biol.250. 223-238 (1996)

    • Description
      「研究成果報告書概要(欧文)」より
  • [Publications] Shiraki, Kentaro: "Trifluoroethanol-induced stabilization of the alpha-helical structure of beta-lactoglobulin" J.Mol.Biol.245. 180-194 (1995)

    • Description
      「研究成果報告書概要(欧文)」より
  • [Publications] Kataoka, Mikio: "Structural characterization of the molten globule and native states of apomyoglobin by solution X-ray scattering" J.Mol.Biol.249. 215-228 (1995)

    • Description
      「研究成果報告書概要(欧文)」より
  • [Publications] Kawata, Yasushi: "The role of ATP hydrolysis in the function of the chaperonin GroEL-Dynamic complex formation with GroES" FEBS Letters. 369. 283-286 (1995)

    • Description
      「研究成果報告書概要(欧文)」より
  • [Publications] Kuwajima, Kunihiro: "The molten globule state of alpha-lactalbumin" FASEB J.10. 102-109 (1996)

    • Description
      「研究成果報告書概要(欧文)」より
  • [Publications] Peng, Zheng-yu: "Local structural preferences in the alpha-lactalbumin molten globule" Biochemistry. 34. 3248-3252 (1995)

    • Description
      「研究成果報告書概要(欧文)」より
  • [Publications] Dill, Ken A.: "Principles of protein folding-A perspective from simple exact models" Protein Sci.4. 561-602 (1995)

    • Description
      「研究成果報告書概要(欧文)」より
  • [Publications] Balbach, Jochen: "Following protein folding in real time using NMR spectroscopy" Nature Struct.Biol.2. 865-870 (1995)

    • Description
      「研究成果報告書概要(欧文)」より
  • [Publications] Shi, Lee: "Conformational characterization of DnaK and its complexes with substrate protein by small-angle X-ray scattering" Biochemistry. 35. 3297-3308 (1996)

    • Description
      「研究成果報告書概要(欧文)」より
  • [Publications] Hamada, Daizo: "Salt-induced formation of the molten globule state of apomyoglobin studied by isothermal titration calorimetry" Thermochimica Acta. 266. 385-400 (1995)

    • Description
      「研究成果報告書概要(欧文)」より

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Published: 1999-03-09  

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