| Title: | "Conformational analysis of the Saccharomyces cerevisiae tridecapeptide mating pheromone by 13C,15N rotational-echo double resonance nuclear magnetic resonance spectroscopy" |
| Author(s): | Garbow JR; Breslav M; Antohi O; Naider F; |
| Address: | "Monsanto Corporate Research, Monsanto Company, St. Louis, Missouri 63198" |
| ISSN/ISBN: | 0006-2960 (Print) 0006-2960 (Linking) |
| Abstract: | "The solid-state conformation of [Nle12]alpha-factor, the Saccharomyces cerevisiae tridecapeptide mating pheromone (WHWLQLKPGQPNleY), was investigated by 13C,15N rotational-echo double resonance (REDOR) nuclear magnetic resonance spectroscopy (NMR). Previous high-resolution NMR studies of [Nle12]alpha-factor in solution revealed a transient Type II beta-turn spanning residues 7-10 of the peptide. To investigate this region of [Nle12]alpha-factor in the solid state, a series of four selectively 13C,15N-enriched tridecapeptides were synthesized by solid-phase methods. Carbon-nitrogen distances between the labeled sites in lyophilized samples of [Nle12]alpha-factor were accurately measured by REDOR NMR. Experimentally determined distances were compared with those from calculated models for Type I and Type II beta-turns and for an extended chain. The measured distances indicate that, in a lyophilized powder, the central region of the [Nle12]alpha-factor is not in an extended conformation. The experimental data was most consistent with distances obtained from a distorted Type I beta-turn model" |
| Keywords: | "Amino Acid Sequence *Magnetic Resonance Spectroscopy Mating Factor Molecular Sequence Data Peptides/*chemistry Protein Conformation Protein Structure, Secondary Saccharomyces cerevisiae/*chemistry;" |
| Notes: | "MedlineGarbow, J R Breslav, M Antohi, O Naider, F eng GM22086/GM/NIGMS NIH HHS/ GM22087/GM/NIGMS NIH HHS/ Research Support, U.S. Gov't, P.H.S. 1994/08/23 Biochemistry. 1994 Aug 23; 33(33):10094-9. doi: 10.1021/bi00199a037" |
