19F NMR studies of the native and denatured states of green fluorescent protein.

@article{Khan200619FNS,
  title={19F NMR studies of the native and denatured states of green fluorescent protein.},
  author={Farid Khan and Ilya Kuprov and Timothy D Craggs and P J Hore and Sophie E. Jackson},
  journal={Journal of the American Chemical Society},
  year={2006},
  volume={128 33},
  pages={10729-37}
}
Biosynthetic preparation and (19)F NMR experiments on uniformly 3-fluorotyrosine-labeled green fluorescent protein (GFP) are described. The (19)F NMR signals of all 10 fluorotyrosines are resolved in the protein spectrum with signals spread over 10 ppm. Each tyrosine in GFP was mutated in turn to phenylalanine. The spectra of the Tyr --> Phe mutants, in conjunction with relaxation data and results from (19)F photo-CIDNP (chemically induced dynamic nuclear polarization) experiments, yielded a… CONTINUE READING