A family of glyprolines, short peptides whose amino acid sequences contain glycine and proline residues, is regulatory peptides. At present, the mechanisms of action of glyprolines 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. The spatial structure and the conformational properties of the natural glyproline tetrapeptide molecule Pro-Gly-Pro-Gly and its analogues Pro-Gly-Pro-Arg, Pro-Gly-Pro-Leu, Pro-Gly-Pro-Val, Pro-Gly-Pro-Phe were investigated using theoretical conformational analysis method. Using this glyproline peptides of the human body, you can create new and effective drugs.The potential energy of the molecule was estimated as the sum of non-valent, electrostatic, torsion interactions and the energy of hydrogen bonds. The low-energy conformations were found for glyproline analogues, 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 these molecules have the folded and half folded types of backbone. These forms bring part of the backbone and the side chains of the amino acids together, and they result in convenient interactions.
conformation, peptide, spatial structure, molecule
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