Трехмерная структура пентапептидной молекулы Arg-Glu-Arg-Gly-Pro

Abstract

It seems relevant to carry out structural and functional studies of glyprolines and their synthetic analogues on model systems using theoretical research methods. Glyprolines are a family of short peptides whose amino acid sequences contain residues of proline and glycine. Currently their mechanisms of action are poorly understood. Great interest in their structure is caused by the possibility of creating new drugs that are the human body’s own reserve. Glyproline molecules are stable and eddicient. Using the method of molecular mechanics, the spatial structure and conformational properties of the glyproline pentapeptide molecule Arg-Glu-Arg-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. 9 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 Arg and Glu 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.