title: [Theoretical studies of the electrostatic interactions in aspartic proteinases, intramolecular interactions in pepsin and penicillopepsin].
abstract: A semi-empirical approach has been used to estimate the intramolecular electrostatic interactions in pepsin and penicillopepsin. The pH-dependence of the free energy electrostatic term was calculated, and the pH-dependence of the domain interactions has been estimated. As it was shown, the contribution of electrostatic interactions is rather small for the stabilization of the native structure. At the same time the electrostatic repulsion between domains increases with the increase of pH. The later can be the cause of the alkaline denaturation of pepsin and domain mobility.
authors.forename: A
authors.initials: A
authors.lastname: Miteva
authors.forename: A
authors.initials: A
authors.lastname: Karshikov
authors.forename: B
authors.initials: B
authors.lastname: Atanasov
authors.forename: A A
authors.initials: AA
authors.lastname: Zhdanov
authors.forename: N S
authors.initials: NS
authors.lastname: Andreeva
mesh_terms: D016282:Aspartic Acid Endopeptidases; D004560:Electricity; D010450:Endopeptidases; D006863:Hydrogen-Ion Concentration; D010434:Pepsin A; D011487:Protein Conformation
chemical_list: D010450:Endopeptidases; C022325:aspartic proteinase A; D016282:Aspartic Acid Endopeptidases; D010434:Pepsin A
vernacular_title: Teoreticheskie issledovaniia élektrostaticheskikh vzaimodeĭstviĭ v aspartatnykh proteinazakh, vnutrimolekuliarnye vzaimodeĭstviia v pepsine i penitsillopepsine.