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Thermodynamic of the reconstitution of protein structure from peptide fragments.

Research Project

Project/Area Number 09680660
Research Category

Grant-in-Aid for Scientific Research (C)

Allocation TypeSingle-year Grants
Section一般
Research Field Biophysics
Research InstitutionKwansei Gakuin University

Principal Investigator

SEGAWA Shin-ichi  Kwansei Gakuin University, School of Science, Professor, 理学部, 教授 (70103132)

Project Period (FY) 1997 – 1999
Project Status Completed (Fiscal Year 1999)
Budget Amount *help
¥3,300,000 (Direct Cost: ¥3,300,000)
Fiscal Year 1999: ¥600,000 (Direct Cost: ¥600,000)
Fiscal Year 1998: ¥500,000 (Direct Cost: ¥500,000)
Fiscal Year 1997: ¥2,200,000 (Direct Cost: ¥2,200,000)
KeywordsCytochrome c / Peptide fragment-complex / Thermodynamics / Protein folding / Calorimetry / チトクロムC / ペプチド断片複合体
Research Abstract

Two peptide fragments from tuna cytochrome c, (1-44)H [H means that the fragment contains heme] and (45-103), combine to from a 1 : 1 fragment complex. This was clearly proved by ion-spray mass spectrometry. CD and NMR spectra showed that the structure of the fragment complex formed is similar to that of on intact cytochrome c, although each isolated fragment itself is unstructured. Binding constants and enthalpies upon the complex formation were directly observed by isothermal titration calorimetry. The change in enthalpy upon the complex formation was somewhat larger than that upon protein folding, because of the electrostatic attractive interactions between the amino group of N-terminus of (45-103) and heme propionates. When the electrostatic force was reduced by the addition of KCI, the enthalpy change become to coincide with each other.
In addition, smaller peptide fragments were prepared to investigate the effect of the losing some peptide segment from the whole amino acid sequence of protein. Prepared peptide fragments were (1-21)H, (22-44), (45-66) and (67-103). Calorimetric and spectroscopic experiments showed that the peptide segment (45-66) is important for the formation of energetically stable structure between N- and C-terminal helices.

Report

(4 results)
  • 1999 Annual Research Report   Final Research Report Summary
  • 1998 Annual Research Report
  • 1997 Annual Research Report
  • Research Products

    (12 results)

All Other

All Publications (12 results)

  • [Publications] Noda Yasuo: "A Two-dimensional NMR study of exchange behavior of amide hydrogens in a Lysozyme derivative with an extra cross-link between Glu35 and Trp108"Biopolymers. 41. 131-143 (1997)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1999 Final Research Report Summary
  • [Publications] Kubo Shigeru: "Improvement in the oxidative folding of endothelin-1 by a Lys-Arg extension at the amino terminus"Letters in Peptide Science. 4. 185-192 (1997)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1999 Final Research Report Summary
  • [Publications] Yokota Atsushi: "Thermodynamics of the reconstitution of tuna Cytochrome c from two peptide fragments"Protein Science. 7. 1717-1727 (1998)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1999 Final Research Report Summary
  • [Publications] Yokota Atsushi: "The transition state in the folding-unfolding reaction of four Species of three-disulfide variant of hen lysozyme"J. Mol. Biol.. 295. 1275-1288 (2000)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1999 Final Research Report Summary
  • [Publications] Noda, Y. , Fukuda, Y. & Segawa, S.: ""A Two-Dimensional NMR Study of Exchange Behavior of Amide Hydrogens in a Lysozyme Derivative with an Extra Cross-Link Between Glu35 and Trp 108""Biopolymers. 41. 131-143 (1997)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1999 Final Research Report Summary
  • [Publications] Kubo, S., Chino, N., Nakajima, K., Aumelas, A., Chiche, L., Segawa, S., Tamaki, H., Kobayashi, Y., Kimura, T. & Sakakibara, S.: ""Improvement in the oxidative folding of endothelin-1 by a Lys-Arg extension at the amino terminus""Letters in Peptide Science. 4. 185-192 (1997)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1999 Final Research Report Summary
  • [Publications] Yokota, A., Takenaka, H., Oh, T., Noda, Y. & Segawa, S.: ""Thermodynamics of the reconstitution of tuna cytochrome c from two peptide fragments""Prptein Science. 7. 1717-1727 (1998)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1999 Final Research Report Summary
  • [Publications] Yokota, A., Izutani, K., Takai, M., Kubo, Y., Noda, Y., Koumoto, Y., Tachibana, H. & Segawa, S.: ""The Transition State in the Folding-Unfolding Reaction of Four Species of Three-disulfide Variant of Hen Lysozyme""J. Mol. Biol.. 295. 1275-1288 (2000)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1999 Final Research Report Summary
  • [Publications] Atsushi Yokota: "Thermodynamics of the Reconstitution of Tuna Cytochrome c from Two Peptide Fragments"Protein Science. 4. 1717-1727 (1998)

    • Related Report
      1999 Annual Research Report
  • [Publications] Atsushi Yokota: "Thermodynamics of the Reconstitution of Tuna Cytochromec from Two Peptide Fragments" Protein Science. 4. 1717-1727 (1998)

    • Related Report
      1998 Annual Research Report
  • [Publications] Noda Yasuo: "A Two-Dimensional NMR Study of Exchange Behavior of Amide Hydrogens in a Lysozyme Denvative with an Extra Cross-Link Between Glu35 and Trp108" Biopolymers. 41. 131-143 (1997)

    • Related Report
      1997 Annual Research Report
  • [Publications] Kubo Shigeru: "Improvement in the oxidative folding of endothelin-1 by a Lys-Arg extension at the amino terminus" Letters in Peptide Science. 4. 185-192 (1997)

    • Related Report
      1997 Annual Research Report

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Published: 1997-04-01   Modified: 2016-04-21  

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