Spatial Structure of Soymorphin-6 Molecule

Possible conformations of the soymorphin-6 molecule (Tyr1–Pro2–Phe3–Val4–Val5–Asn6—NH₂) have been studied by theoretical conformational analysis. The potential function of the system was chosen as the sum of nonvalent, electrostatic and torsion interactions and the energy of hydrogen bonds. Low-energy conformations of the soymorphin-6 molecule have been found, the values of the dihedral angles of the main and side chains of amino-acid residues that make up the molecule, and the energy of intra- and inter-residual interactions has been estimated. It was shown that the spatial structure of the soymorphin-6 molecule is represented by conformations of eight shapes of the peptide skeleton. The results we obtained can be used to elucidate the structural and structural-functional organization of soymorphins.