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Structure-Function Analysis of One single Ferritin Molecule with Electron Microscopy

Research Project

Project/Area Number 08455378
Research Category

Grant-in-Aid for Scientific Research (B)

Allocation TypeSingle-year Grants
Section一般
Research Field 生物・生体工学
Research InstitutionNational Institute for Physiological Sciences (1997)
The University of Tokyo (1996)

Principal Investigator

NAGAYAMA Kuniaki  National Institute for Physiological Sciences, Ultrastructure Research, Professor, 生理学研究所, 教授 (70011731)

Co-Investigator(Kenkyū-buntansha) TAKAHASHI Takuya  National Institute for Physiological Sciences, Ultrastructure Research, Research, 生理学研究所, 助手 (70262102)
Project Period (FY) 1996 – 1997
Project Status Completed (Fiscal Year 1997)
Budget Amount *help
¥6,500,000 (Direct Cost: ¥6,500,000)
Fiscal Year 1997: ¥3,100,000 (Direct Cost: ¥3,100,000)
Fiscal Year 1996: ¥3,400,000 (Direct Cost: ¥3,400,000)
KeywordsElectron microscopy / Ferritin / Structure-function relation / Single molecular analysis / Biophysics / 構造・機能相関 / 生物物理学
Research Abstract

This research was planned to establish a functional assay for a single protein molecule. To recognize individual protein molecules, electron microscopy, which is the most prominent in the spacial resolving power, was employed. As the biological function recognizable with electron microscopy, we have chosen the iron-incorporation process conducted by ferritin molecules, which could store iron of up to 3500 atoms, easily identified with the mirosocpy, For the two-years research duration, following new findings were obtained.
1)A single molecular functional assay of iron-incorporatibility of ferritin is established with TEM and high resolution SEM
2)Ferritin molecules stably adsorbed onto silicon surface shows about 20% residual function on iron-incorporability compared with those in the solution phase
3)Low on high pH condition drastically impairs the iron-incorporation activity of ferritin molecules when stably adsorbed onto silicon surface
4)Anti-correction between the functional stability and the strength of adsorption is observed
5)Ferritin molecules transfered from the mercury surface to the carbon surface in keeping the array form can maintain the iron-incorporability up to 85%.
6)The closely packed array form of ferritin molecules are very stable in maintaing activity compared with those sparsely and randomly adsorbed on carbon surface.

Report

(3 results)
  • 1997 Annual Research Report   Final Research Report Summary
  • 1996 Annual Research Report
  • Research Products

    (7 results)

All Other

All Publications (7 results)

  • [Publications] 永山国昭(編): "“Protein Array : An Alternative Biomolecular System" Advances in Biophysies Vol.34" 学会出版センター, 350 (1997)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1997 Final Research Report Summary
  • [Publications] 永山国昭(編): ""Protein Array : An Alternative Biomolecular System" Advanced in Biophysics Vol.34" 学会出版センター, 350 (1997)

    • Related Report
      1997 Annual Research Report
  • [Publications] E.Adachi and K.Nagayama: "Formation of Holo ferritin Hexagonal Array in Secondary Films Due to Alder type transition" Langmuir. 109. 1836-1839 (1996)

    • Related Report
      1996 Annual Research Report
  • [Publications] N.Denkov,H.Yoshimura and K.Nagayama: "Method for controlled formation of vitrified films for cryo-electron microscopy" Ultramicroscopy. 65. 147-158 (1996)

    • Related Report
      1996 Annual Research Report
  • [Publications] N.Denkov,H.Yoshimura and K.Nagayama: "Nanoparticle Array in Freely Suspended Vitrified Films" Phys Rev.Lett.2354-2357 (1996)

    • Related Report
      1996 Annual Research Report
  • [Publications] K.Nagayama: "Protein Array Engineering" Supramol.Sci.3. 363-374 (1996)

    • Related Report
      1996 Annual Research Report
  • [Publications] 永山国昭(編): ""Protein Array"Advances in Biophysics" 学会出版センター, 350 (1997)

    • Related Report
      1996 Annual Research Report

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Published: 1996-04-01   Modified: 2016-04-21  

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