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Issue 27, 2013
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Quantitative comparison of protein dynamics in live cells and in vitro by in-cell 19F-NMR

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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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Publication details

The article was received on 25 Dec 2012, accepted on 12 Feb 2013 and first published on 14 Feb 2013


Article type: Communication
DOI: 10.1039/C3CC39205H
Citation: 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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