Membrane protein structural studies predominantly rely on  detergent micelles to mimic cell membranes. However,  a lack of understanding of the physical properties required for a micelle to stabilize a membrane protein fold and function significantly hinders these investigations. Currently, detergents are empirically screened and not rationally selected. One physical property of interest is micelle fluidity and how the dynamics of the micelles effect membrane protein fold and activity. To quantify micelle dynamics, spin labeled lipids were doped into various detergent micelles at a ratio of one lipid per micelle and the dynamics were quantified using EPR spectroscopy. In addition, the fluidity of the micelles with additives such as cholic-acid derivatives were also investigated. The results suggest that, in addition to modulating micelle shapes and sizes, fluidity can be modulated with binary mixtures increasing the controllable physical properties of micelles for membrane protein investigations.

Modulating detergent micelle fluidity for membrane protein structural studies

246th National Meeting (2013)

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