[Thermodynamic and kinetic study of thermal denaturation of Kunitz soybean trypsin inhibitor by differential scanning microcalorimetry].
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.
Varfolomeeva
E P
EP
Burova
T V
TV
Grinberg
V Ia
VIa
Tolstoguzov
V B
VB
D002152:Calorimetry, Differential Scanning; D007700:Kinetics; D011489:Protein Denaturation; D013816:Thermodynamics; D014360:Trypsin Inhibitor, Kunitz Soybean / Q000032:analysis*; D014361:Trypsin Inhibitors / Q000032:analysis*
D014361:Trypsin Inhibitors; D014360:Trypsin Inhibitor, Kunitz Soybean
Termodinamicheskoe i kineticheskoe issledovanie termicheskoĭ denaturatsii ingibitora tripsina Kunitsa iz bobov soi medodom differentsial'noĭ skaniruiushcheĭ mikrokalorimetrii.