[Interpretation of thermograms of protein denaturation in non-equilibrium conditions].
Data are presented concerning the effect of heating rate on the denaturation parameters of small and oligomeric globular proteins: Kunitz trypsin inhibitor from soybeans and 1,5-Ribulose Bisphosphate Carboxylase from tobacco leaves. Substantional dependence of denaturation temperature on the heating rate reflects non-equilibrium pattern of denaturation of these proteins under experimental conditions. To interpret these data a kinetic approach is proposed, which permits determination of equilibrium value of the denaturation temperature and of the constant of de- and renaturation rate. The conformation transitions in the proteins studied are shown to be relatively slow processes. Their rate is comparable to the velocity of temperature change in a calorimeter, which is the cause of non-equilibrium effects in a calorimetric experiment.
Burova
T V
TV
Varfolomeeva
E P
EP
Grinberg
V Ia
VIa
Suchkov
V V
VV
Papkov
V S
VS
Bauve
Kh
Kh
Tolstoguzov
V B
VB
D002151:Calorimetry; D006358:Hot Temperature; D007700:Kinetics; D008433:Mathematics; D008962:Models, Theoretical; D010947:Plants, Toxic; D011489:Protein Denaturation; D012273:Ribulose-Bisphosphate Carboxylase / Q000032:analysis; D014026:Nicotiana / Q000201:enzymology; D014360:Trypsin Inhibitor, Kunitz Soybean / Q000032:analysis
D014360:Trypsin Inhibitor, Kunitz Soybean; D012273:Ribulose-Bisphosphate Carboxylase
K voprosu ob interpretatsii termogramm denaturatsii belkov v neravnovesnykh usloviiakh.