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This research aims to explore localized conformational dynamics in proteins using genetically encoded pentafluorophenylalanine and F NMR.

Genetically Encoded Pentafluorophenylalanine Enables Quantitative Probing of Local Protein Malleability by ¹⁹ F NMR

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This research aims to explore localized conformational dynamics in proteins using genetically encoded pentafluorophenylalanine and F NMR.
Utilized F NMR to measure ring-flip kinetics quantitatively
Investigated various proteins to assess ring-flip rates and conformational changes
Conducted pressure-dependent experiments to analyze activation volumes and assess allosteric modulation
Ring-flip rates varied significantly within the same hydrophobic cluster, indicating localized fluctuations
Small activation volumes suggest spatial confinement of structural rearrangements during ring flips
Ligand binding affected ring-flip rates site-specifically, revealing allosteric effects on protein dynamics.

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Randomized trial demonstrates how local protein malleability is probed using F NMR, suggesting new engineering strategies.

Paul et al. (2026) studied this question.

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