title: [An objective method for isolating globular protein domains].
abstract: Regions of more stability and nearest environs were localized on the basis 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 included into one domain and residues from l+1 to l+1+m are included into another domain. According to this criterium, the boundary between two domains is set between two residues in the case when the interaction energy is minimal when first residue is included into the first domain and the second one into another. Structural domains are founded and probability of existing of domains boundary is studied for the binase, barnase, and complex of barnase with dioxy-dinucleotide inhibitor. It is determinated that the biggest structural interaction between domains coinsiders with location of domains at 1-43, 44-110 residues correspondently.
authors.forename: I N
authors.initials: IN
authors.lastname: Berezovskiĭ
authors.forename: V G
authors.initials: VG
authors.lastname: Tumanian
mesh_terms: D001426:Bacterial Proteins; D004722:Endoribonucleases / Q000737:chemistry; D004791:Enzyme Inhibitors / Q000737:chemistry; D009711:Nucleotides / Q000737:chemistry; D011506:Proteins / Q000737:chemistry*; D012260:Ribonucleases / Q000037:antagonists & inhibitors / Q000737:chemistry
chemical_list: D001426:Bacterial Proteins; D004791:Enzyme Inhibitors; D009711:Nucleotides; D011506:Proteins; D004722:Endoribonucleases; D012260:Ribonucleases; C019760:Bacillus amyloliquefaciens ribonuclease; C022543:ribonuclease T(2)