AN OBJECTIVE METHOD FOR LOCALIZATION OF D OMAINS IN GLOBULAR-PROTEINS

Regions of more stability and nearest environs were localized on the b asis of the calculation of intramolecular interactions in the frame of pair-wise approach. A criterium for definition of domains boundary in globular proteins is establishing if residues from k to l are include d into one domain and residues from l+1 to l+1+m are included into ano ther domain. According to this criterium, the boundary between two dom ains is set between two residues in the case when the interaction ener gy is minimal when first residue is included into the first domain and the second one into another. Structural domains are founded and proba bility of existing of domains boundary is studied for the binase, barn ase, and complex of barnase with dioxy-dinucleotide inhibitor. It is d eterminated that the bigest structural interaction between domains coi nsiders with location of domains at 1-43, 44-110 residues corresponden tly.