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 language | English |
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Pages (from-to) | 2801-2803 |
Number of pages | 3 |
Journal | Chemical Communications |
Volume | 49 |
Issue number | 27 |
DOIs | |
Publication status | Published - 2013 Mar 7 |
Externally published | Yes |
ASJC Scopus subject areas
- Catalysis
- Electronic, Optical and Magnetic Materials
- Ceramics and Composites
- Chemistry(all)
- Surfaces, Coatings and Films
- Metals and Alloys
- Materials Chemistry