title: GroEL provides a folding pathway with lower apparent activation energy compared to spontaneous refolding of human carbonic anhydrase II.
abstract: The kinetics of the refolding of the enzyme, human carbonic anhydrase II (HCA II), at different temperatures, together with the Escherichia coli chaperonin GroEL, has been studied. The Arrhenius plots for the spontaneous, GroEL-assisted, and GroEL/ES-assisted refolding of HCA II show that the apparent activation energy (E(a)) is lower in the presence of the chaperonin GroEL alone than for the spontaneous reaction, whereas the apparent activation energy for the GroEL/ES-assisted reaction is almost the same as for the spontaneous reaction (85, 46, and 72 kJ/mol, for the spontaneous, GroEL, and GroEL/ES-assisted reactions, respectively).
authors.affiliation: IFM/Department of Chemistry, Linköping University, Sweden.
authors.forename: M
authors.initials: M
authors.lastname: Persson
authors.forename: U
authors.initials: U
authors.lastname: Carlsson
authors.forename: N
authors.initials: N
authors.lastname: Bergenhem
mesh_terms: D002256:Carbonic Anhydrases / Q000378:metabolism*; D018834:Chaperonin 60 / Q000502:physiology*; D004793:Enzyme Reactivators; D006801:Humans; D017510:Protein Folding; D013696:Temperature; D013816:Thermodynamics
chemical_list: D018834:Chaperonin 60; D004793:Enzyme Reactivators; D002256:Carbonic Anhydrases