(1)H and (13)C MAS NMR evidence for pronounced ligand-protein interactions involving the ionone ring of the retinylidene chromophore in rhodopsin.

@article{Creemers20021HA,
  title={(1)H and (13)C MAS NMR evidence for pronounced ligand-protein interactions involving the ionone ring of the retinylidene chromophore in rhodopsin.},
  author={Alain F L Creemers and Suzanne R Kiihne and Petra H. M. Bovee-Geurts and Willem J DeGrip and Johan Lugtenburg and Huub J M de Groot},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2002},
  volume={99 14},
  pages={9101-6}
}
Rhodopsin is a member of the superfamily of G-protein-coupled receptors. This seven alpha-helix transmembrane protein is the visual pigment of the vertebrate rod photoreceptor cells that mediate dim light vision. In the active binding site of this protein the ligand or chromophore, 11-cis-retinal, is covalently bound via a protonated Schiff base to lysine residue 296. Here we present the complete (1)H and (13)C assignments of the 11-cis-retinylidene chromophore in its ligand-binding site… CONTINUE READING