Issue 27, 2013
From the journal:

Chemical Communications

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

Yousuke Takaoka,a   Yoshiyuki Kioi,a   Akira Morito,b   Junji Otani,b   Kyohei Arita,b   Eishi Ashihara,c   Mariko Ariyoshi,b   Hidehito Tochio,b   Masahiro Shirakawab  and  Itaru Hamachi*ad  

* Corresponding authors

a Department of Synthetic Chemistry and Biological Chemistry, Graduate School of Engineering, Kyoto University, Katsura, Nishikyo-ku, Kyoto, Japan
E-mail: ihamachi@sbchem.kyoto-u.ac.jp
Fax: +81-75-383-2759
Tel: +81-75-383-2754

b Department of Molecular Engineering, Graduate School of Engineering, Kyoto University, Katsura, Nishikyo-ku, Kyoto, Japan

c Department of Clinical and Translational Physiology, Kyoto Pharmaceutical University, 5 Nakauchi, Yamashina-ku, Kyoto, Japan

d Core Research for Evolutional Science and Technology (CREST), JST, 5 Sanbancho, Chiryoda-ku, Tokyo, Japan

Abstract

Here we describe how a 19F-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.

Graphical abstract: Quantitative comparison of protein dynamics in live cells and in vitro by in-cell 19F-NMR

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Article information

DOI
https://doi.org/10.1039/C3CC39205H
Article type
Communication
Submitted
25 Dec 2012
Accepted
12 Feb 2013
First published
14 Feb 2013

Chem. Commun., 2013,49, 2801-2803

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

Y. Takaoka, Y. Kioi, A. Morito, J. Otani, K. Arita, E. Ashihara, M. Ariyoshi, H. Tochio, M. Shirakawa and I. Hamachi, Chem. Commun., 2013, 49, 2801 DOI: 10.1039/C3CC39205H

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