| Title: | Conformation of a biologically active C-terminal hexapeptide analog of the pheromone biosynthesis activating neuropeptide by NMR spectroscopy |
| Author(s): | Wang YS; Kempe TG; Raina AK; Mazzocchi PH; |
| Address: | "Department of Chemistry and Biochemistry, University of Maryland, College Park" |
| DOI: | 10.1111/j.1399-3011.1994.tb00391.x |
| ISSN/ISBN: | 0367-8377 (Print) 0367-8377 (Linking) |
| Abstract: | "The solution conformation of a biologically active C-terminal hexapeptide analog of the pheromone biosynthesis activating neuropeptide Tyr-D-Phe-Ser-Pro-Arg-Leu-NH2 has been studied by NMR spectroscopy. A beta-turn conformation was identified from the NOE connectivities observed for the peptide in a mixed solvent of water and DMSO, indicating that this is the biologically active conformation of the peptide. This study also suggests that the use of such an aqueous-like solvent mixture allows the observation of a preferred conformation for small linear peptides in the presence of conformational averaging" |
| Keywords: | "Amino Acid Sequence Dimethyl Sulfoxide Magnetic Resonance Spectroscopy/methods Molecular Sequence Data Neuropeptides/*chemistry Oligopeptides/chemical synthesis/*chemistry Protein Conformation Protein Structure, Secondary Sex Attractants/chemical synthesi;" |
| Notes: | "MedlineWang, Y S Kempe, T G Raina, A K Mazzocchi, P H eng Denmark 1994/03/01 Int J Pept Protein Res. 1994 Mar; 43(3):277-83. doi: 10.1111/j.1399-3011.1994.tb00391.x" |
