Spatial structure of the ovalulin molecule

The conformational possibilities of the ovalulin (Tyr1-Pro2-Leu3-Asp4-Leu5-Phe6-OH) molecule were studied by theoretical conformational analysis. The potential function of the system is chosen as the sum of non-valence, electrostatic, and torsion interactions and the energy of hydrogen bonds. The low-energy conformations of the ovalulin molecule, the dihedral angles of the main and side chains of the amino acid residues that make up the molecule were found, and the energy of intra- and inter-residual interactions was estimated. It has been shown that the spatial structure of the ovalulin molecule is represented by conformations of eight shapes of the peptide skeleton. The results obtained can be used to elucidate the structural and structural-functional organization of the ovalulin molecule.