Leveraging relaxation-optimized 1H–13CF correlations in 4-19F-phenylalanine as atomic beacons for probing structure and dynamics of large proteins

Nature Chemistry, Published online: 05 May 2025; doi:10.1038/s41557-025-01818-8

Correlating aromatic carbons attached to fluorine with meta-position hydrogens in fluorine-labelled phenylalanines can yield two-dimensional correlations with narrow linewidths in large proteins. Adapting phenylalanine-tRNA synthetase increases the incorporation rate, while expanding the genetic code enables site-specific incorporation of fluorinated phenylalanine. The resulting HCF-transverse relaxation-optimized spectroscopy can illuminate protein dynamics and drive multiplexed drug discovery campaigns.

​Nature Chemistry, Published online: 05 May 2025; doi:10.1038/s41557-025-01818-8Correlating aromatic carbons attached to fluorine with meta-position hydrogens in fluorine-labelled phenylalanines can yield two-dimensional correlations with narrow linewidths in large proteins. Adapting phenylalanine-tRNA synthetase increases the incorporation rate, while expanding the genetic code enables site-specific incorporation of fluorinated phenylalanine. The resulting HCF-transverse relaxation-optimized spectroscopy can illuminate protein dynamics and drive multiplexed drug discovery campaigns. Read More

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