Hydrophobic core of molten-globule state of bovine carbonic anhydrase B.
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.
Mitaku
S
S
Tokyo University of Agriculture and Technology, Faculty of Technology, Japan.
Ishido
S
S
Hirano
Y
Y
Itoh
H
H
Kataoka
R
R
Saitô
N
N
D000818:Animals; D002256:Carbonic Anhydrases / Q000737:chemistry*; D002417:Cattle; D002942:Circular Dichroism; D005456:Fluorescent Dyes; D011487:Protein Conformation; D011721:Pyrenes; D013050:Spectrometry, Fluorescence
D005456:Fluorescent Dyes; D011721:Pyrenes; C030984:pyrene; D002256:Carbonic Anhydrases