Measurement of dipolar couplings in a transducin peptide fragment weakly bound to oriented photo-activated rhodopsin.

@article{Koenig2000MeasurementOD,
  title={Measurement of dipolar couplings in a transducin peptide fragment weakly bound to oriented photo-activated rhodopsin.},
  author={Bernd W. Koenig and Drake C. Mitchell and Steffen Koenig and Stephan Grzesiek and Burton J. Litman and Adriaan Bax},
  journal={Journal of biomolecular NMR},
  year={2000},
  volume={16 2},
  pages={121-5}
}
Rhodopsin-containing disks, isolated from rod outer segments of bovine retina, align at high magnetic fields with their membrane normal parallel to the magnetic field. After light-activation of rhodopsin, transient binding of the C-terminal transducin undecapeptide, selectively labeled with 15N at Leu5 and Gly9, results in residual dipolar contributions to the 1J(NH) splittings for these two residues. Both residues show 1J(NH) splittings which are smaller than in the dark-adapted or rhodopsin… CONTINUE READING

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