title: [Study of trypsin-substrate and trypsin-inhibitor complexes. 1. Conformation of Asp-102, His-57 and Ser-195 residues in the trypsin active center].
abstract: Using the semi-empirical method of conformational analysis low energetic conformations were found for trypsin's catalytic triad Asp102, His57, Ser195 in the field of the active centre that consisted of about 800 atoms. It was shown that within the enzyme structure conformations which are preferential for isolated residues are formed. Lability obtained for the side chains is in accord with their functions in enzymatic catalysis. Results of the calculations carried out correlate with the X-ray data for trypsin complexes.
mesh_terms: D000494:Allosteric Regulation; D000595:Amino Acid Sequence; D001224:Aspartic Acid; D001665:Binding Sites; D006639:Histidine; D011487:Protein Conformation; D012694:Serine; D014357:Trypsin; D014361:Trypsin Inhibitors
chemical_list: D014361:Trypsin Inhibitors; D001224:Aspartic Acid; D012694:Serine; D006639:Histidine; D014357:Trypsin
vernacular_title: Izuchenie tripsin-substratnogo i tripsin-ingibitornogo kompleksov. 1. Konformatsiia ostatkov Asp-102, His-57 i Ser-195 activnogo tsentra tripsina.