Abstract
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.
MeSH terms
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Benzenesulfonamides
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Carbonic Anhydrase I / chemistry
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Carbonic Anhydrase I / metabolism
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Crystallography, X-Ray
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Erythrocytes / metabolism*
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Fluorine Radioisotopes*
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Hemoglobins / chemistry
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Hemoglobins / metabolism
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Humans
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Ligands
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Magnetic Resonance Spectroscopy*
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Models, Molecular
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Protein Conformation
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Proteins / chemistry*
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Proteins / metabolism
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Sulfonamides / metabolism
Substances
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Fluorine Radioisotopes
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Hemoglobins
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Ligands
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Proteins
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Sulfonamides
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Carbonic Anhydrase I