The conformation of a-factor is not influenced by the S-prenylation of Cys12.

Abstract

Two-Dimensional NMR was used to examine the solution conformation of the lipopeptide a-factor, YIIKGVFWDPAC (S-farnesyl) OCH3, from the yeast Saccharomyces cerevisiae and five analogues containing various S-alkylated cysteines in DMSO-d6. NOESY data, NH temperature coefficients, and 3J alpha NH coupling constants indicate that the a-factor is a predominantly unstructured peptide in DMSO. Similar results were obtained for the other peptides indicating that S-prenylation of Cys12 does not affect the conformation of these peptides.

Cite this paper

@article{Gounarides1991TheCO, title={The conformation of a-factor is not influenced by the S-prenylation of Cys12.}, author={J S Gounarides and Michelle S. Broido and C B Xue and Jeffrey M. Becker and Fred R. Naider}, journal={Biochemical and biophysical research communications}, year={1991}, volume={181 3}, pages={1125-30} }