Quantitative comparison of protein dynamics in live cells and in vitro by in-cell (19)F-NMR.

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

Chemical communications (Cambridge, England) 2013 Apr 07

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Here we describe how a (19)F-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.

Citation

Yousuke Takaoka, Yoshiyuki Kioi, Akira Morito, Junji Otani, Kyohei Arita, Eishi Ashihara, Mariko Ariyoshi, Hidehito Tochio, Masahiro Shirakawa, Itaru Hamachi. Quantitative comparison of protein dynamics in live cells and in vitro by in-cell (19)F-NMR. Chemical communications (Cambridge, England). 2013 Apr 07;49(27):2801-3