[Surface potential energy of peptides and conformation of amino acid residues in proteins. Preliminary results of processing using databank protein structures].

The fact of enzymatic synthesis of a protein polypeptide chain have been mentioned. The potential energy surfaces of peptides have been analysed. Based on the obtained results and characteristic peculiarity of the enzymatic reactions have been concluded that the non-glycine residues in a three-dimensional (3-D) protein structure most likely should be in the negative conformations. The analysis of the amino acid residue conformations have been performed on the 185 3-D protein structures obtained by the X-ray crystallography at high resolution. It has been shown that the changes in the protein surrounding environment, in crystalline forms and functional state of protein, bindings of the ligands and inhibitors do not lead to the changes in the polarity of non-glycine residues conformational angles phi, and in the polarity of the conformational angles omega of all residues. Based on the results, 81 independent protein structures have been selected. The preliminary results of analysis of glycine and non-glycine residue conformations occurring in these structures have been presented.