The conformation of a-factor is not influenced by the S-prenylation of Cys12.
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.
Gounarides
J S
JS
Department of Chemistry, Hunter College, New York, NY.
Broido
M S
MS
Xue
C B
CB
Becker
J M
JM
Naider
F R
FR
D000215:Acylation; D000595:Amino Acid Sequence; D003545:Cysteine; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D000072235:Mating Factor; D008745:Methylation; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*; D010675:Pheromones / Q000737:chemistry; D011487:Protein Conformation; D013329:Structure-Activity Relationship
D010455:Peptides; D010675:Pheromones; D000072235:Mating Factor; D003545:Cysteine