Small-angle neutron scattering studies of protein-reversed micelle complexes.

Enzymes solubilized in organic solvents, hosted within the polar cores of surfactant aggregates, known as reversed micelles, provide many unique opportunities for new biocatalytic synthesis and protein separation processes. Small-angle neutron scattering (SANS) studies have shown that insertion of the protein cytochrome-c in the reversed micelle polar core causes a significant reapportioning of the surfactants and water between the filled and unfilled micelles, leading to an increase in overall size of the filled micelles relative to their empty counterparts. The simple shell and core model assuming single occupancy of the reversed micelles has significant limitations in interpreting data for high protein loadings, and points to the need for more detailed characterization of the protein-reversed micelle interactions.