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Related Concept Videos

Protein Dynamics in Living Cells01:19

Protein Dynamics in Living Cells

Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...

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Visualizing and Braking Protein Ring Flips with Difluorotyrosines.

Meng Lu1,2, Wenkai Zhu1,2, Guohua Xu1,2

  • 1State Key Laboratory of Magnetic Resonance Spectroscopy and Imaging, National Center for Magnetic Resonance in Wuhan, Innovation Academy for Precision Measurement Science and Technology, Chinese Academy of Sciences, Wuhan 430071, P. R. China.

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|July 9, 2026
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Summary

Fluorine-19 NMR quantifies protein ring-flip dynamics using novel probes. These probes, 3,5-difluorotyrosine and 2,6-difluorotyrosine, enable measurement and modulation of these essential biological motions.

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Area of Science:

  • Biochemistry
  • Biophysics
  • Chemical Biology

Background:

  • Protein "breathing" motions, including aromatic ring flips, are crucial for biological functions.
  • Quantifying and controlling these dynamics, especially within living cells, presents significant challenges.

Purpose of the Study:

  • To develop and apply 19F NMR for measuring aromatic ring-flip dynamics on the microsecond to second timescale.
  • To utilize novel difluorotyrosine probes to detect and modulate tyrosine ring flips in proteins.
  • To investigate the influence of cellular environments on ring-flip dynamics.

Main Methods:

  • Employing fluorine-19 Nuclear Magnetic Resonance (19F NMR) spectroscopy.
  • Synthesizing and utilizing cost-effective 3,5-difluorotyrosine (3,5-F2Y) and 2,6-difluorotyrosine (2,6-F2Y) probes.
  • Measuring ring-flip timescales (τflip) in proteins like ubiquitin, GB1, and HPr under various conditions, including macromolecular crowding.

Main Results:

  • Detected previously unobserved tyrosine ring flips in ubiquitin with τflip ≈ 15 μs using 19F NMR.
  • Demonstrated that 3,5-F2Y acts as a minimally perturbing probe for ring-flip dynamics.
  • Showed that 2,6-F2Y effectively inhibits ring flips, reducing their rate by approximately 10^3-fold in GB1 and HPr.
  • Evaluated the impact of macromolecular crowding and intracellular conditions on ring-flip dynamics.

Conclusions:

  • 19F NMR is a powerful technique for quantifying aromatic ring-flip dynamics across various timescales.
  • Difluorotyrosine probes offer versatile tools for both measuring and modulating protein ring-flip motions.
  • This approach provides new strategies for studying and controlling protein dynamics in vitro and within living cellular systems.