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Hydrophobic core of molten-globule state of bovine carbonic anhydrase B
1Tokyo University of Agriculture and Technology, Faculty of Technology, Japan.
Biophysical Chemistry
|July 1, 1991
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.