Abstract
Hydrated reversed micelles of Aerosol OT (AOT) in octane have been studied by 13C NMR spectroscopy. The changes of spin-lattice relaxation times (T1) for individual segments of the AOT molecule, induced by entrapping a protein (α-chymotrypsin) into the micelle, have been determined by the inversion-recovery technique. The dramatic (three-fold) increase of T1 found for the α-CH2 groups in the AOT molecules indicates that (unlike in the unfilled micelle) in the protein-containing micelle the boundary of the water cavity is shifted outward (0.5-0.7 nm, under the given experimental conditions), the alkyl chains of the surfactant being “flooded” by water molecules. This observation explains why the outer size of the reversed micelle does not change on insertion of a bulky protein molecule.
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