title: 'All-or-none' mechanism of the molten globule unfolding.
abstract: The Gdm-HCl-induced unfolding of bovine carbonic anhydrase B and S. aureus beta-lactamase was studied at 4 degrees C by a variety of methods. With the use of FPLC it has been shown that within the transition from the molten globule to the unfolded state the distribution function of molecular dimensions is bimodal. This means that equilibrium intermediates between the molten globule and the unfolded states are absent, i.e. the molten globule unfolding follows the 'all-or-none' mechanism.
authors.affiliation: Institute of Protein Research, Russian Academy of Sciences, Moscow.
authors.forename: V N
authors.initials: VN
authors.lastname: Uversky
authors.forename: G V
authors.initials: GV
authors.lastname: Semisotnov
authors.forename: R H
authors.initials: RH
authors.lastname: Pain
authors.forename: O B
authors.initials: OB
authors.lastname: Ptitsyn
mesh_terms: D002256:Carbonic Anhydrases / Q000737:chemistry* / Q000187:drug effects; D002850:Chromatography, Gel; D003080:Cold Temperature; D004305:Dose-Response Relationship, Drug; D019791:Guanidine; D006146:Guanidines / Q000494:pharmacology; D008956:Models, Chemical; D011489:Protein Denaturation; D017510:Protein Folding; D001618:beta-Lactamases / Q000737:chemistry* / Q000187:drug effects
chemical_list: D006146:Guanidines; D001618:beta-Lactamases; D002256:Carbonic Anhydrases; D019791:Guanidine