Abstract
We have synthesized and purified a 19-amino acid peptide whose sequence is derived from the carboxyl-terminal region of bovine rhodopsin, in which the seven serines and threonines that would normally become phosphorylated have been substituted with cysteic acid. The peptide was synthesized by the Fmoc (DCC/HOBl)' procedure using Fmoc-(S-4-methoxytrityl) Cys {Fmoc-Cys(Mmt)-OH}. The Mmt group was removed and the resin-bound peptide was oxidized with performic acid, which also removed other blocking grou_psand cleaved the peptide from the resin.