title: [Thermodynamic and kinetic study of thermal denaturation of Kunitz soybean trypsin inhibitor by differential scanning microcalorimetry].
abstract: The thermal denaturation of soybean trypsin inhibitor (Kunitz inhibitor) has been studied in pH-region from 2.0 to 11.0 by differential scanning microcalorimetry. The thermodynamic characteristics have been determined. It has been established that the denaturation transition of protein may be described by a two-state model. It has been shown, that two side hydrogen bonds between carboxylate-ion and tyrosyl and carboxylate-ion and lysyl take part in the stabilization of the inhibitor's native structure. The activation of denaturation is accompanied by cleavage of one side hydrogen bond.
authors.forename: E P
authors.initials: EP
authors.lastname: Varfolomeeva
authors.forename: T V
authors.initials: TV
authors.lastname: Burova
authors.forename: V Ia
authors.initials: VIa
authors.lastname: Grinberg
authors.forename: V B
authors.initials: VB
authors.lastname: Tolstoguzov
mesh_terms: D002152:Calorimetry, Differential Scanning; D007700:Kinetics; D011489:Protein Denaturation; D013816:Thermodynamics; D014360:Trypsin Inhibitor, Kunitz Soybean / Q000032:analysis*; D014361:Trypsin Inhibitors / Q000032:analysis*
chemical_list: D014361:Trypsin Inhibitors; D014360:Trypsin Inhibitor, Kunitz Soybean
vernacular_title: Termodinamicheskoe i kineticheskoe issledovanie termicheskoĭ denaturatsii ingibitora tripsina Kunitsa iz bobov soi medodom differentsial'noĭ skaniruiushcheĭ mikrokalorimetrii.