| Title: | The conformation of a-factor is not influenced by the S-prenylation of Cys12 |
| Author(s): | Gounarides JS; Broido MS; Xue CB; Becker JM; Naider FR; |
| Address: | "Department of Chemistry, Hunter College, New York, NY" |
| Journal Title: | Biochem Biophys Res Commun |
| DOI: | 10.1016/0006-291x(91)92055-o |
| ISSN/ISBN: | 0006-291X (Print) 0006-291X (Linking) |
| 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" |
| Keywords: | Acylation Amino Acid Sequence Cysteine Magnetic Resonance Spectroscopy/methods Mating Factor Methylation Molecular Sequence Data Peptides/*chemistry Pheromones/chemistry Protein Conformation Structure-Activity Relationship; |
| Notes: | "MedlineGounarides, J S Broido, M S Xue, C B Becker, J M Naider, F R eng GM22086/GM/NIGMS NIH HHS/ GM22087/GM/NIGMS NIH HHS/ GM46520/GM/NIGMS NIH HHS/ Comparative Study Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. 1991/12/31 Biochem Biophys Res Commun. 1991 Dec 31; 181(3):1125-30. doi: 10.1016/0006-291x(91)92055-o" |
