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Structural Studies of Macromolecules in Solution using Small Angle X-Ray Scattering
Published on: November 5, 2018
Small-angle neutron scattering studies of protein-reversed micelle complexes
E Sheu1, K E Göklen, T A Hatton
1Massachusetts Institute of Technology Cambridge, MA 02139.
Biotechnology Progress
|June 23, 2010
Summary
Enzymes in reversed micelles offer new biocatalytic synthesis options. Protein insertion alters micelle structure, necessitating advanced models for high protein concentrations.
Area of Science:
- Biocatalysis
- Supramolecular Chemistry
- Protein Engineering
Background:
- Enzymes in organic solvents, within reversed micelles, enable novel biocatalytic synthesis and protein separation.
- Reversed micelles are surfactant aggregates with polar cores, capable of solubilizing enzymes.
Purpose of the Study:
- To investigate the structural changes in reversed micelles upon protein (cytochrome-c) insertion.
- To evaluate the applicability of current models for describing protein-micelle interactions at high protein loadings.
Main Methods:
- Small-angle neutron scattering (SANS) was employed to study the size and structure of reversed micelles.
- Protein (cytochrome-c) was incorporated into reversed micelles to observe its effect on the system.
Main Results:
- Protein insertion caused significant redistribution of surfactants and water between micelles.
- Filled micelles showed an increased size compared to empty micelles.
- A simple shell and core model was insufficient for high protein loadings.
Conclusions:
- Protein-micelle interactions within reversed micelles are complex and lead to structural rearrangements.
- Advanced characterization methods are required to accurately model protein-reversed micelle systems, especially at high concentrations.
