title: Modeling of irreversible thermal protein denaturation at varying temperature. II. The complete kinetic model of Lumry and Eyring.
abstract: 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 zero, has been considered. The theoretical dependences of excess heat capacity on temperature have been constructed. The variation of the shape of the theoretical curves with varied values of the enthalpy change for the second step, Arrhenius equation parameters for both steps, and the scanning rate has been studied.
authors.affiliation: Bach Institute of Biochemistry, Russian Academy of Sciences, Moscow, 117071, Russia. inbio@glas.apc.org.
authors.forename: A E
authors.initials: AE
authors.lastname: Lyubarev
authors.forename: B I
authors.initials: BI
authors.lastname: Kurganov
mesh_terms: D004926:Escherichia coli / Q000201:enzymology; D007700:Kinetics; D008956:Models, Chemical; D011489:Protein Denaturation; D013696:Temperature; D013816:Thermodynamics; D014543:Uridine Phosphorylase / Q000737:chemistry
chemical_list: D014543:Uridine Phosphorylase