Quantitative comparison of protein dynamics in live cells and in vitro by in-cell19F-NMR

Yousuke Takaoka, Yoshiyuki Kioi, Akira Morito, Junji Otani, Kyohei Arita, Eishi Ashihara, Mariko Ariyoshi, Hidehito Tochio, Masahiro Shirakawa, Itaru Hamachi

Research output: Contribution to journalArticle

28 Citations (Scopus)

Abstract

Here we describe how a19F-probe incorporated into an endogenous protein by a chemical biology method revealed protein dynamics. By explicit determination of ligand-bound and unbound structures with X-ray crystallography, the quantitative comparison of the protein's dynamics in live cells and in vitro is presented. These results clearly demonstrated the greater conformational fluctuations of the intracellular protein, partially due to macromolecular crowding effects.

Original languageEnglish
Pages (from-to)2801-2803
Number of pages3
JournalChemical Communications
Volume49
Issue number27
DOIs
Publication statusPublished - 2013 Mar 7
Externally publishedYes

ASJC Scopus subject areas

  • Catalysis
  • Electronic, Optical and Magnetic Materials
  • Ceramics and Composites
  • Chemistry(all)
  • Surfaces, Coatings and Films
  • Metals and Alloys
  • Materials Chemistry

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  • Cite this

    Takaoka, Y., Kioi, Y., Morito, A., Otani, J., Arita, K., Ashihara, E., Ariyoshi, M., Tochio, H., Shirakawa, M., & Hamachi, I. (2013). Quantitative comparison of protein dynamics in live cells and in vitro by in-cell19F-NMR. Chemical Communications, 49(27), 2801-2803. https://doi.org/10.1039/c3cc39205h