Study of the binding environment of alpha-factor in its G protein-coupled receptor using fluorescence spectroscopy.

@article{Ding2002StudyOT,
  title={Study of the binding environment of alpha-factor in its G protein-coupled receptor using fluorescence spectroscopy.},
  author={F X Ding and B K Lee and Melinda Hauser and R Patri and Boris Arshava and Jeffrey M. Becker and Fred R. Naider},
  journal={The journal of peptide research : official journal of the American Peptide Society},
  year={2002},
  volume={60 1},
  pages={65-74}
}
Mating in Saccharomyces cerevisiae is induced by the interaction of alpha-factor (W1H2W3L4Q5L6K7P8G9Q10P11M12Y13) with its cognate G protein-coupled receptor (Ste2p). Fifteen fluorescently labeled analogs of alpha-factor in which the 7-nitrobenz-2-oxa-1,3-diazol-4-yl (NBD) group was placed at the alphaN-terminus and in side-chains at positions 1, 3, 4, 6, 7, 12 and 13 were synthesized and assayed for biological activity and receptor affinity. Eleven of the analogs retained 6-60% of the… CONTINUE READING