title: [Evaluation of the energy of the stabilization of the transitional state due to hydrogen bonds in the active site of serine proteases].
abstract: Using the semiempirical MNDO method, several systems simulating the active site of serine proteases have been studied. The stabilization energy was found to depend strongly on the nucleophilicity of the attacking group. The decrease of the activation energy has been estimated as 9 kcal/mole. It was shown that the substrate distortion does not vary with forming of hydrogen bonds.
mesh_terms: D001665:Binding Sites; D002384:Catalysis; D006860:Hydrogen Bonding; D008954:Models, Biological; D009211:Myoglobin / Q000031:analogs & derivatives* / Q000032:analysis; D011789:Quantum Theory; D012697:Serine Endopeptidases
chemical_list: D009211:Myoglobin; C055547:deoxymyoglobin; D012697:Serine Endopeptidases
vernacular_title: Otsenka énergii stabilizatsii perekhodnogo sostoianiia za schet vodorodnykh sviazeĭ v aktivnom tsentre serinovykh proteaz.