What question did this study set out to answer?

To develop a transverse relaxation-optimized NMR method using fluorinated 13C aromatic spin pairs to overcome line broadening and signal attenuation in large proteins.

May 5, 2025Nature ChemistryOpen Access

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

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To develop a transverse relaxation-optimized NMR method using fluorinated 13C aromatic spin pairs to overcome line broadening and signal attenuation in large proteins.
Synthesized [4-19F13Cζ; 3,5-2H2ε] Phe engineered with specific relaxation and spin–spin coupling properties.
Incorporated the engineered residue globally via adapted phenylalanine-tRNA synthetase and site-specifically via genetic code expansion into proteins spanning 30 kDa to 180 kDa.
Recorded two-dimensional 1H–13CF correlation spectra using transverse relaxation-optimized spectroscopy (TROSY) selection without requiring 19F-dedicated probes.
Generated two-dimensional NMR correlation spectra with sharply narrowed linewidths across proteins ranging from 30 kDa to 180 kDa.
Enabled high-resolution small-molecule ligand interaction studies on large macromolecular systems using conventional NMR hardware.
Achieved both global residue-specific and site-specific genetic encoding of fluorinated phenylalanine probes.

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Implication

In vitro biophysical study demonstrates narrow NMR linewidths in 30–180 kDa proteins via 1H–13CF TROSY, suggesting expanded capabilities for large macromolecular drug discovery.

Cite This Study

Boeszoermenyi et al. (2025) studied this question.

synapsesocial.com/papers/6a775b8fa7498e5110ae80ef https://doi.org/10.1038/s41557-025-01818-8

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Implication

In vitro biophysical study demonstrates narrow NMR linewidths in 30–180 kDa proteins via 1H–13CF TROSY, suggesting expanded capabilities for large macromolecular drug discovery.

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

Key Points

Discussion

Implication

Cite This Study

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

Key Points

Discussion

Implication

Cite This Study

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