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We consider in this work the analysis of the excess heat capacity C(p)(ex) versus temperature profiles in terms of a model of thermal protein denaturation involving one irreversible step. It is shown that the dependences of ln C(p)(ex) on 1 T (T is the absolute temperature) obtained at various temperature scanning rates have the same form. Several new(More)
The thermal stability of rabbit skeletal muscle glycogen phosphorylase b was characterized using enzymological inactivation studies, differential scanning calorimetry, and analytical ultracentrifugation. The results suggest that denaturation proceeds by the dissociative mechanism, i.e., it includes the step of reversible dissociation of the active dimer(More)
Thermal denaturation of creatine kinase from rabbit skeletal muscle has been studied by differential scanning calorimetry. The excess heat capacity vs. temperature profiles were independent of protein concentration, but strongly temperature scanning rate-dependent. It has been shown that thermal denaturation of creatine kinase satisfies the previously(More)
Thermal denaturation of uridine phosphorylase from Escherichia coli K-12 has been studied by differential scanning calorimetry. The excess heat capacity vs. temperature profiles were obtained at temperature scanning rates of 0.25, 0.5, and 1 K/min. These profiles were analysed using three models of irreversible denaturation which are approximations to the(More)
We propose a spatial structure for the tricarboxylic acid cycle enzyme complex (tricarboxylic acid cycle metabolon). The structure is based on an analysis of data on the interaction between tricarboxylic acid cycle enzymes and the mitochondrial inner membrane, as well as on data on enzyme-enzyme interactions. The alpha-ketoglutarate dehydrogenase complex,(More)
In a number of metabolic pathways enzyme concentrations are comparable to those of substrates. Recently it has been shown that many statements of the 'classical' metabolic control theory are violated if such a system contains a moiety-conserved cycle. For arbitrary pathways we have found: (a) the equation connecting coefficients CEiJ (obtained by varying(More)
Protein stability plays an extremely important role not only in its biological function but also in medical science and protein engineering. Osmolytes provide a general method to protect proteins from the unfolding and aggregation induced by extreme environmental stress. In this study, the effect of glycerol on protection of the model enzyme creatine kinase(More)
The problems of the origin of life and biochemical evolution are analyzed in the context of the biochemical organization concept proposed earlier by the authors. The traditional view according to which the evolution of biological systems occurred from lower levels to systems of higher levels is criticized. It is suggested that the formation of the cell and(More)
The model of thermal protein denaturation involving two consecutive irreversible steps has been analyzed. The equation describing the dependence of excess heat capacity (Cpex) on temperature (T) under a constant scanning rate has been obtained and used for construction of theoretical Cpex versus T profiles. The change in the shape of theoretical profiles at(More)
The model for thermal denaturation of proteins involving consecutive reversible and irreversible steps (Lumry and Eyring model) has been analyzed. The most general case, when equilibrium in the first step is established slowly in comparison with the rate of the second step and the heat effect value for the second step is either greater than or less than(More)