Rational design of 19F NMR labelling sites to probe protein structure and interactions
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Abstract
Proteins are investigated in increasingly more complex biological systems, where 19 F NMR is proving highly advantageous due to its high gyromagnetic ratio and background-free spectra. Its application has, however, been hindered by limited chemical shift dispersions and an incomprehensive relationship between chemical shifts and protein structure. Here, we exploit the sensitivity of 19 F chemical shifts to ring currents by designing labels with direct contact to a native or engineered aromatic ring. Fifty protein variants predicted by AlphaFold and molecular dynamics simulations show 80–90% success rates and direct correlations of their experimental chemical shifts with the magnitude of the engineered ring current. Our method consequently improves the chemical shift dispersion and through simple 1D experiments enables structural analyses of alternative conformational states, including ribosome-bound folding intermediates, and in-cell measurements of protein-protein interactions and thermodynamics. Our strategy thus provides a simple and sensitive tool to extract residue contact restraints from chemical shifts for previously intractable systems.
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FRETpredict: a Python package for FRET efficiency predictions using rotamer libraries
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Structures of protein folding intermediates on the ribosome
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Structures of protein folding intermediates on the ribosome
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Self-citationLu, S., Wu, Q. Y., Wang, S., Sun, D., Liu, Y., Huang, S., & Huang, B. (2025) · Analytical Chemistry · doi:10.1021/acs.analchem.5c05583 · Cited by 8 · see citing works
Long-range electrostatic forces govern how proteins fold on the ribosomePreprint
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Self-citationBurridge, C., & Burmann, B. M. (2026) · Chemistry - Methods · doi:10.1002/cmtd.202500155 · Cited by 1 · see citing works
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NMR Studies on Protein–Ligand Interactions
Yao, H., & Xu, N. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27177561
Synthesis and In Vivo Incorporation of 4‐Difluoromethyl‐L‐Phenylalanine Into Proteins
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Shi, P., Liang, J., Liu, X., Zhang, Y., Shi, C., Guo, S., Song, J., Tian, C., & Li, C. (2026) · Journal of the American Chemical Society · doi:10.1021/jacs.6c12448
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Introduction to the principles of protein engineering
Sharp, J. F., Nelson, M. K., Rustembek, M., Samanta, R., & Stern, L. A. (2026) · Elsevier eBooks · doi:10.1016/b978-0-443-44536-1.00010-9
Su, Z., Li, S., Wu, X., & Huang, S. (2026) · Analytical Chemistry · doi:10.1021/acs.analchem.6c05927
- Authors
- Streit, J. O., Chan, S. H. S., Daya, S., & Christodoulou, J.
- Affiliations
- Institute of Structural and Molecular Biology (GB)
- Corresponding author
- Streit, Julian O.
- Chan, Sammy H. S.
- Christodoulou, John
- Venue
- Nature Communications
- Published
- 2025-05-08
- Volume
- 16
- Issue
- 1
- Pages
- 4300-4300
- ISSN
- 2041-1723 (ISSN-L)
- PMC
- PMC12062419
- OpenAlex
- W4410203739
- Cited by
- 17
- References
- 98
- Citations by year
- 2026: 15 · 2025: 2
- FWCI
- 4.30
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Nature Communications (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- UCL Discovery (University College London) (submittedVersion)
- Funders
- Wellcome Trust (206409/Z/17/Z)
- Topics
- Physical Sciences › Chemistry › Spectroscopy › Advanced NMR Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biophysics › Electron Spin Resonance Studies
- Keywords
- 19F NMR chemical shifts, ring current, protein structure determination, protein-protein interaction, folding intermediates, ribosome, conformational states
- MeSH terms
- Fluorine, Magnetic Resonance Spectroscopy, Protein Binding, Protein Conformation, Proteins, Thermodynamics, Protein Folding, Nuclear Magnetic Resonance, Biomolecular, Molecular Dynamics Simulation
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