Abstract
Micelle-forming detergents are used to solubilize integral membrane proteins for biochemical and physical characterizations. However, the unique properties of each membrane protein require exhaustive, and currently empirical, screening to optimize the detergent conditions which yield a stable protein-detergent complex (PDC). Detergent mixtures provide a means of expanding the available micellar environments, while also allowing select properties of micelles to be engineered. The properties of detergent mixtures must be well understood to correlate these properties with the stability of the protein fold and function. Using small-angle X-ray scattering, we determined the sizes and shapes of micelles formed by a comprehensive set of commercially available detergents commonly used with membrane proteins, and systematically assessed binary mixtures of these detergents. Micelle size and shape were determined directly from a Guinier analysis of the low angle data, the position of the second maxima at intermediate angles, and a core-shell model fit to the micelle scattering profiles. Many micelle properties, such as hydrophobic thickness, have a linear dependence on the micelle mole fraction. In addition to modulating the size of the micelle, other properties such as surface charge and fluidity can also be engineered. The results of this investigation can now be used to rationally design micelles for membrane protein investigations.
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