title: [Spatial structure of the cardioactive octapeptide].
abstract: The spatial structure of the cardioactive octapeptide Pro1-Gln2-Asp3-Pro4-Phe5-Leu6-Arg7-Ile8-NH2 was investigated using the theoretical conformational analysis. The low-energy conformations of the octapeptide molecule were found, the values of dihedral angles of the backbone and side chains of the amino acid residues constituting the peptide were determined, and the energies of intra-and interresidual interactions were estimated. It was shown that the spatial structure of this molecule represent six stable low-energy forms of the main chain.
authors.forename: L I
authors.initials: LI
authors.lastname: Ismailova
authors.forename: R M
authors.initials: RM
authors.lastname: Abbasly
authors.forename: N A
authors.initials: NA
authors.lastname: Akhmedov
mesh_terms: D008958:Models, Molecular; D009842:Oligopeptides / Q000737:chemistry*; D011487:Protein Conformation; D013816:Thermodynamics
chemical_list: D009842:Oligopeptides