SEGMENTAL MOBILITY OF MOLECULES IN THE REVERSED MICELLES OF AEROSOL OT IN N-OCTANE CONTAINING ALPHA-CHYMOTRYPSIN AND ALBUMINстатья
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Аннотация:Spin-lattice relaxation times (T1) measured by C-13 NMR spectroscopy of surfactant molecules in the colloid systems formed by Aerosol OT (AOT) in cyclohexane with of without alpha-chymotrypsin and albumin in aqueous microphase at different surfactant (cyclohexane) water ratios have been studied as a characteristic of segmental mobility of the surfactant. Incorporation of the proteins in the reversed micelles of AOT is followed by elimination of excess water from the inner cavity into the hydrophobic area within a separate microphase rather than an increase of the size of the cavity. Upon the entrappment of alpha-chymotrypsin, the aqueous phase is displaced into the hydrophobic zone by 5-7 angstrom, and of albumin - by 8-10 angstrom. When the hydration degree is increased, one molecule of alpha-chymotrypsin and two molecules of albumin can be incorporated into the micelle of AOT. The magnetic non-equivalency of C-13 nuclei of different alkyl - fragments of AOT systems from their different packing densities in a micelle as a result of a close contact of the carbonyl of (CH2)CO-fragment with SO3-group and distant contacting with the carbonyl of (CH)CO-fragment. The conclusion is also supported by the application of the hydrophilic paramagnetic probe. On hydration of the reversed micelles, a conformational rearrangement of alkyl chains in the vicinity of the polar fragment of the molecule of AOT proceeds, followed by an increase of the contribution of gauche-forms. The rearrangement assumes the displacement of water molecules as a separate phase on encapsulation of protein molecules that is supported in the experiment. The morphology of biocatalytic assemblies may determine their activity and mechanisms of interaction with a substrate in the processes of micellar enzymology and in the structure of biological membranes.