Posttranslational, site-directed photochemical fluorine editing of protein sidechains to probe residue oxidation state via19F-nuclear magnetic resonance

Patrick G. Isenegger, Brian Josephson, Ben Gaunt, Matthew J. Davy, Veronique Gouverneur, Andrew J. Baldwin, Benjamin G. Davis

Published: 2023-02-19 DOI: 10.1038/s41596-022-00800-9

photochemical fluorination

protein sidechains

19F-NMR

site-directed modification

oxidation state probe

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The fluorination of amino acid residues represents a near-isosteric alteration with the potential to report on biological pathways, yet the site-directed editing of carbon–hydrogen (C–H) bonds in complex biomolecules to carbon–fluorine (C–F) bonds is chal
Introduction
Materials
Procedure
- Formation of histone eH3.1-Dha4
- Photochemical mutagenesis—formation of histone eH3.1-γF2Met4
Timing
Troubleshooting
Anticipated results
- References
References
ACKNOWLEDGMENTS

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Posttranslational, site-directed photochemical fluorine editing of protein sidechains to probe residue oxidation state via19F-nuclear magnetic resonance

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