Deformation dynamics of fluorescent donor-acceptor proteins using time resolved ultra fast FRET spectroscopy

DOI 9 References
  • Baba Motoyoshi
    Institute for Solid State Physics, University of Tokyo
  • Suzuki Masayuki
    Institute for Solid State Physics, University of Tokyo
  • Ganeev Rashid
    Institute for Solid State Physics, University of Tokyo
  • Kuroda Hiroto
    Institute for Solid State Physics, University of Tokyo
  • Ozaki Tsuneyuki
    Institut national de la recherche scientifique - Energie, Materiaux et Telecommunication
  • Hamakubo Takao
    Laboratory for System Biology and Medicine, Research Center for Advanced Science and Technology, University of Tokyo
  • Masuda Kazuyuki
    Laboratory for System Biology and Medicine, Research Center for Advanced Science and Technology, University of Tokyo
  • Hayashi Masahiro
    Laboratory for System Biology and Medicine, Research Center for Advanced Science and Technology, University of Tokyo
  • Sakihama Toshiko
    Laboratory for System Biology and Medicine, Research Center for Advanced Science and Technology, University of Tokyo
  • Kodama Tatsuhiko
    Laboratory for System Biology and Medicine, Research Center for Advanced Science and Technology, University of Tokyo
  • Kozasa Tohru
    Department of Pharmacology, College of Medicine, University of Illinois

Bibliographic Information

Other Title
  • ＦＲＥＴ（Ｆｌｕｏｒｅｓｃｅｎｃｅ　Ｒｅｓｏｎａｎｃｅ　Ｅｎｅｒｇｙ　Ｔｒａｎｓｆｅｒ）分光法における蛋白機能性の出現機構

Description

We measured the decay time shortening of the FRET(Fluorescence Resonance Energy Transfer) signals in a mixed donor-acceptor protein pair such as the cameleon calcium ion indicator and a ligand activated GRIN-Go proteins pair with a newly improved an ultra fast time-resolved FRET spectroscopy system using photon counting method in this study. G protein-coupled receptors is the most important protein family for the recognition of many chemical substances at the cell surface. For both protein pair systems, donor CFP protein fluorescence lifetime curves showed the double decay and the fluorescence lifetime distinctly shortened in the FRET condition. Simultaneously we got the emission spectral distribution of luminous protein within 10ns from excitation, which is the first data acquired time-resolvedly at the initial stage in the FRET condition. This system enables us to trace the dynamics of the interaction between proteins at the ligand induced activated state, molecular structure change and combination or dissociation.

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Details 詳細情報について

  • CRID
    1390282679743528832
  • NII Article ID
    130004491965
  • DOI
    10.2530/jslsm.26.315
  • ISSN
    18811639
    02886200
  • Text Lang
    ja
  • Data Source
    • JaLC
    • Crossref
    • CiNii Articles
  • Abstract License Flag
    Disallowed

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