Conformation of a biologically active C-terminal hexapeptide analog of the pheromone biosynthesis activating neuropeptide by NMR spectroscopy.
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.
Wang
Y S
YS
Department of Chemistry and Biochemistry, University of Maryland, College Park.
Kempe
T G
TG
Raina
A K
AK
Mazzocchi
P H
PH
D000595:Amino Acid Sequence; D004121:Dimethyl Sulfoxide; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008969:Molecular Sequence Data; D009479:Neuropeptides / Q000737:chemistry*; D009842:Oligopeptides / Q000138:chemical synthesis / Q000737:chemistry*; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D012724:Sex Attractants / Q000138:chemical synthesis / Q000737:chemistry; D012996:Solutions; D014867:Water
D009479:Neuropeptides; D009842:Oligopeptides; D012724:Sex Attractants; D012996:Solutions; C079709:pheromone biosynthesis activating neuropeptide, Helicoverpa zea; D014867:Water; D004121:Dimethyl Sulfoxide