title: Hydrophobic core of molten-globule state of bovine carbonic anhydrase B.
abstract: The interaction which stabilizes the intermediate state of the protein folding and/or unfolding is important for understanding the structure formation mechanism of proteins. The partitioning of a hydrophobic fluorescence probe, pyrene, into the core of a 'molten globule' structure of bovine carbonic anhydrase B was measured, revealing a partition coefficient of about 10(4). The result leads to the conclusion that the compact structure of the molten-globule state is formed by the hydrophobic interaction, as detergent micelles are formed by the same interaction.
authors.affiliation: Tokyo University of Agriculture and Technology, Faculty of Technology, Japan.
authors.forename: S
authors.initials: S
authors.lastname: Mitaku
authors.forename: S
authors.initials: S
authors.lastname: Ishido
authors.forename: Y
authors.initials: Y
authors.lastname: Hirano
authors.forename: H
authors.initials: H
authors.lastname: Itoh
authors.forename: R
authors.initials: R
authors.lastname: Kataoka
authors.forename: N
authors.initials: N
authors.lastname: Saitô
mesh_terms: D000818:Animals; D002256:Carbonic Anhydrases / Q000737:chemistry*; D002417:Cattle; D002942:Circular Dichroism; D005456:Fluorescent Dyes; D011487:Protein Conformation; D011721:Pyrenes; D013050:Spectrometry, Fluorescence
chemical_list: D005456:Fluorescent Dyes; D011721:Pyrenes; C030984:pyrene; D002256:Carbonic Anhydrases