In‐Cell <sup>19</sup>F NMR of Proteins: Recent Progress and Future Opportunities

Chai, Zhaofei; Li, Conggang

doi:10.1002/chem.202303988

Cited by 5 publications

References 76 publications

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Fluorinated Tags to Study Protein Conformation and Interactions Using ¹⁹F NMR

Hanson,

Coxon

2024

ChemBioChem

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The incorporation of fluorine atoms into a biomacromolecule provides a background‐free and environmentally sensitive reporter of structure, conformation and interactions using 19F NMR. There are several methods to introduce the 19F reporter – either by synthetic incorporation via solid phase peptide synthesis; by suppressing the incorporation or biosynthesis of a natural amino acid and supplementing the growth media with a fluorinated counterpart during protein expression; and by genetic code expansion to add new amino acids to the amino acid alphabet. This review aims to discuss progress in the field of introducing fluorinated handles into biomolecules for NMR studies by post‐translational bioconjugation or ‘fluorine‐tagging’. We will discuss the range of chemical tagging ‘warheads’ that have been used, explore the applications of fluorine tags, discuss ways to enhance reporter sensitivity and how the signal to noise ratios can be boosted. Finally, we consider some key challenges of the field and offer some ideas for future directions.

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Fluorinated Tags to Study Protein Conformation and Interactions Using ¹⁹F NMR

Hanson,

Coxon

2024

ChemBioChem

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Synthesis of hexafluorovaline-containing di- and tripeptides

Bellucci,

Romani,

Sani

et al. 2024

Journal of Fluorine Chemistry

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Insights into the Structure and Dynamics of Proteins from ¹⁹F Solution NMR Spectroscopy

Sengupta

2024

Biochemistry

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19 F NMR spectroscopy has recently witnessed a resurgence as an attractive analytical tool for the study of the structure and dynamics of biomolecules in vitro and in cells, despite reports of its applications in biomolecular NMR since the 1970s. The high gyromagnetic ratio, large chemical shift dispersion, and complete absence of the spin 1/2 19 F nucleus from biomolecules results in background-free, highresolution 19 F NMR spectra. The introduction of 19 F probes in a few selected locations in biomolecules reduces spectral crowding despite its increased line width in comparison to typical 1 H NMR line widths and allows rapid site-specific measurements from simple 1D spectra alone. The design and synthesis of novel 19 F probes with reduced line widths and increased chemical shift sensitivity to the surrounding environment, together with advances in labeling techniques, NMR methodology, and hardware, have overcome several drawbacks of 19 F NMR spectroscopy. The increased interest and widespread use of 19 F NMR spectroscopy of biomolecules is gradually establishing it as a sensitive and high-resolution probe of biomolecular structure and dynamics, supplementing traditional 13 C/ 15 Nbased methods. This Review focuses on the advances in 19 F solution NMR spectroscopy of proteins in the past 5 years, with an emphasis on novel 19 F tags and labeling techniques, NMR experiments to probe protein structure and conformational dynamics in vitro, and in-cell NMR applications.

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In‐Cell ¹⁹F NMR of Proteins: Recent Progress and Future Opportunities

Cited by 5 publications

References 76 publications

Fluorinated Tags to Study Protein Conformation and Interactions Using ¹⁹F NMR

Fluorinated Tags to Study Protein Conformation and Interactions Using ¹⁹F NMR

Synthesis of hexafluorovaline-containing di- and tripeptides

Insights into the Structure and Dynamics of Proteins from ¹⁹F Solution NMR Spectroscopy

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In‐Cell 19F NMR of Proteins: Recent Progress and Future Opportunities

Cited by 5 publications

References 76 publications

Fluorinated Tags to Study Protein Conformation and Interactions Using 19F NMR

Fluorinated Tags to Study Protein Conformation and Interactions Using 19F NMR

Synthesis of hexafluorovaline-containing di- and tripeptides

Insights into the Structure and Dynamics of Proteins from 19F Solution NMR Spectroscopy

Contact Info

Product

Resources

About

In‐Cell ¹⁹F NMR of Proteins: Recent Progress and Future Opportunities

Fluorinated Tags to Study Protein Conformation and Interactions Using ¹⁹F NMR

Fluorinated Tags to Study Protein Conformation and Interactions Using ¹⁹F NMR

Insights into the Structure and Dynamics of Proteins from ¹⁹F Solution NMR Spectroscopy