Spatial Structure of The Rubiscolin-6 Molecule

The conformational possibilities of the rubiscolin-6 molecule (Tyr1-Pro2-Leu3-Asp4-Leu5-Phe6-NH2) were investigated using theoretical conformational analysis. The potential function of the system was chosen as the sum of non-bonded, electrostatic, and torsional interactions, as well as hydrogen bond energy. Low-energy conformations of the rubiscolin-6 molecule were found, with values of dihedral angles for the main and side chains of the amino acid residues involved in the molecule's structure, and the energy of intra- and inter-residue interactions was assessed. It was shown that the spatial structure of the rubiscolin-6 molecule consists of conformations of eight shapes of the peptide backbone. The results obtained may be used to investigate the structural and structure-function organization of the rubiscolin-6 molecule.