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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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Article information


Submitted
25 Dec 2012
Accepted
12 Feb 2013
First published
14 Feb 2013

Chem. Commun., 2013,49, 2801-2803
Article type
Communication

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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