Regulatory peptides include the family of glyprolines, short peptides whose amino acid sequences contain glycine and proline residues. Currently, the mechanisms of action of glyprolines are poorly understood. It is possible to understand the mechanisms of their action if we solve the problem of their structural and functional organization. Therefore, the study of the spatial structure of peptides, its ability to change its conformation when interacting with other molecules is an important and actual problem of molecular biophysics. It should be noted that the action of glyprolines is highly stable, fast and efficient. It seems relevant to carry out structural and functional studies of synthetic analogues of glyprolines on model systems using theoretical research methods. Using the method of molecular mechanics, the spatial structure and conformational proper-ties of the glyproline pentapeptide molecule Arg-Pro-Pro-Gly-Phe were determined. The potential energy of this molecule was estimated as the sum of non-valent, electrostatic, torsion interactions and the energy of hydrogen bonds. 10 low-energy conformations of this molecule and the values of the dihedral angles of the main and side chains were found. The energy of the intra- and inter-residue interactions was estimated. The calcu-lation showed that semi-folded forms of the main chain are low-energy for the pen-tapeptide. The side chains of amino acids Arg and Phe in low-energy conformations carry out effective interactions and are conformationally labile amino acids; they bring together the main chain and side chains of the amino acids included in the pentapep-tide.