Calculation of Heat Capacity Changes in Enzyme Catalysis and Ligand Binding.

ABSTRACT: It has been suggested that heat capacity changes in enzyme catalysis may be the underlying reason for temperature optima that are not related to unfolding of the enzyme. If this were to be a common phenomenon, it would have major implications for our interpretation of enzyme kinetics. In most cases, the support for the possible existence of a nonzero (negative) activation heat capacity, however, only relies on fitting such a kinetic model to experimental data. It is therefore of fundamental interest to try to use computer simulations to address this issue. One way is simply to calculate the temperature dependence of the activation free energy and determine whether the relationship is linear or not. An alternative approach is to calculate the absolute heat capacities of the reactant and tra

SUBMITTER: Aqvist J 

PROVIDER: S-EPMC9558309 | biostudies-literature | 2022 Oct

REPOSITORIES: biostudies-literature