[The effect of distribution of adjacent amino acids in primary structures on the possibility of mutation substitutions in globular proteins].

Frequency distributions of adjacent ARs in the primary structures of 320 globular proteins out of different superfamilies were investigated. ARs of every type were compared with the occurrence frequencies of 20 canonic residues at the distances of 1-20 residues according to their primary structure. Amino acid residues were found to be divided into groups of interchangeable residues in the course of globular protein evolution according to the distribution kinds and in terms of Euclidean distances. The use of pancreatic RNases of mammals showed that the approximate preservation of frequency adjacent (1-4 residues according to their primary structure) and characteristics in 5-15 residues mid-interactions may be used in studying the supposed amino acid substitutions in globular protein.