Regulatory peptides include a family of glyprolines, short peptides whose amino acid sequences contain glycine and proline residues. At present, the mechanisms of action of glyprolines and their targets are poorly understood. An important task is also the creation of synthetic analogues of glyprolines, the molecules of which are distinguished by high stability and efficiency. It seems relevant to carry out structural and functional studies of glyprolines and their synthetic analogues on model systems using theoretical research methods. Using the method of molecular mechanics, the spatial structure and conformational properties of the glyproline pentapeptide molecule Thr-Lys-Pro-Gly-Pro were determined. The potential energy of the molecule was estimated as the sum of non-valent, electrostatic, torsion interactions and the energy of hydrogen bonds. 7 low-energy conformations were found for glyproline pentapeptide, the values of structure the dihedral angles of the main and side chains, and the energy of intra-and inter-residue interactions was estimated. It is revealed that low energy conformations of this molecule have the half-folded type of backbone. The side chains of the Thr and Lys amino acids in low-energy conformations carry out effective interactions and are conformationally labile amino acids, they bring together the regions of the main chain and the side chains of the amino acids included in the pentapeptide.