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Analysis of Early Secodary Structure in Globular-Protein Folding.

Research Project

Project/Area Number 60580217
Research Category

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

Allocation TypeSingle-year Grants
Research Field 生物物性学
Research InstitutionHokkaido University

Principal Investigator

KUWAJIMA Kunihiro  Dept. of Polymer Sci., Instructor, Faculty of Sci., Hokkaido Univ., 理学部, 助手 (70091444)

Co-Investigator(Kenkyū-buntansha) NITTA Katsutoshi  Dept. of Polymer Sci., Lecturer, Faculty of Sci., Hokkaido Univ., 理学部, 講師 (80001858)
Project Period (FY) 1985 – 1986
Project Status Completed (Fiscal Year 1986)
Budget Amount *help
¥1,600,000 (Direct Cost: ¥1,600,000)
Fiscal Year 1986: ¥200,000 (Direct Cost: ¥200,000)
Fiscal Year 1985: ¥1,400,000 (Direct Cost: ¥1,400,000)
KeywordsFolding Reaction / CD Spectrum / Stopped-Flow / Lysozyme / <alpha> -Lactalbumin / Parvalbumin / Cytochrome c / β-ラクトグロブリン
Research Abstract

In order to investigate whether the presence of a transient intermediate that has folded secondary structure is a general phenomenon in globular-protein folding or not, kinetic refolding reactions of various proteins have been studied by stopped-flow circular dichroism (CD). Refolding reactions were induced by concentration jumps of guanidine hydrochloride from the unfolded to the native conditions, and resulting CD changes in peptide and side-chain regions were monitored. In all the proteins examined, i.e., lysozyme, <alpha> -lactalbumin, parvalbumin, ferricytochrome c and <beta> -lactoglobulin, there was rapid formation of secondary structure, within the dead time of the stopped-flow apparatus, before the formation of specific tertiary structure. Therefore, there is a transient intermediate formed early in the folding. In lysozyme and <alpha> -lactalbumin, their transient intermediates are similar to each other as expected from their structural homology and also essentially identical to the equilibrium unfolding intermediate of <alpha> -lactalbumin. In parvalbumin and cytochrome c, the transient intermediates have <alpha> -helical structure as expected from their structural patterns in the native state. A <beta> -structural protein, <beta> -lactoglobulin also shows a transient accumulation of the intermediate that involves <beta> -structure, comparable to the structure in the native protein, but also contains an excess of <alpha> -helix. From these results, it is concluded that the protein folding occurs in a hierarchical mechanism in which the framework of secondary structure is restored at an early stage of the reaction.

Report

(1 results)
  • 1986 Final Research Report Summary
  • Research Products

    (10 results)

All Other

All Publications (10 results)

  • [Publications] 桑島邦博,春島嘉章,須貝新太郎: Int.J.Peptide Protein Res.27. 18-27 (1986)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1986 Final Research Report Summary
  • [Publications] 池口雅道,桑島邦博,須貝新太郎: J.Biochem.99. 1191-1201 (1986)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1986 Final Research Report Summary
  • [Publications] 池口雅道,桑島邦博,三谷尚洋,須貝新太郎: Biochemistry. 25. 6965-6972 (1986)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1986 Final Research Report Summary
  • [Publications] 三谷尚洋,春島嘉章,桑島邦博,池口雅道,須貝新太郎: J.Biol.Chem.261. 8824-8829 (1986)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1986 Final Research Report Summary
  • [Publications] 浜野真城,新田勝利,桑島邦博,須貝新太郎: J.Biochem.100. 1617-1622 (1986)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1986 Final Research Report Summary
  • [Publications] Kuwajima, K., Harushima, Y. and Sugai, S.: "Influence of <Ca^(2+)> Binding on the Structure and Stability of Bovine <alpha> -Lactalbumin Studied by Circular Dichroism and Nuclear Magnetic Resonance Spectra." Int. J. Peptide Protein Res.27. 18-27 (1986)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1986 Final Research Report Summary
  • [Publications] Ikeguchi, M., Kuwajima, K. and Sugai, S.: " <Ca^(2+)> -Induced Alteration in the Unfolding Behavior of <alpha> -Lactalbumin." J. Biochem.99. 1191-1201 (1986)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1986 Final Research Report Summary
  • [Publications] Ikeguchi, M., Kuwajima, K., Mitani, M. Sugai, S.: "Evidence for Identity between the Equilibrium Unfolding Intermediate and a Transient Folding Intermediate: A Comparative Study of the Folding Reactions of <alpha> -Lactalbumin and Lysozyme." Biochemistry. 25. 6965-6972 (1986)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1986 Final Research Report Summary
  • [Publications] Mitani, M., Harushima, Y., Kuwajima, K., Ikeguchi, M. and Sugai, S.: "Innocuous Character of [Ethylenebis(oxyethylenenitrilo)]tetraacetic Acid and EDTA as Metal-Ion Buffers in Studying <Ca^(2+)> Binding by <alpha> -Lactalbumin." J. Biol. Chem.261. 8824-8829 (1986)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1986 Final Research Report Summary
  • [Publications] Hamano, M., Nitta, K., Kuwajima, K. and Sugai, S.: "Binding Strength of <Ca^(2+)> Ion to Bovine <alpha> -Lactalbumin." J. Biochem.100. 1617-1622 (1986)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1986 Final Research Report Summary

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Published: 1987-03-31   Modified: 2016-04-21  

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