Due to their unique structure, detergents can act as excellent solubilizing agents. They have a polar, hydrophilic (water-loving) head group which extends from a long hydrophobic (water-fearing) tail. In aqueous solutions, the hydrophilic heads interact with the hydrogen bonds of the water molecules while the hydrophobic tails aggregate to form highly organized spherical structures called micelles upon reaching a certain concentration (known as the Critical Micelle Concentration or CMC). In non-aqueous solutions, detergents form reverse micelles instead.
The average size and shape of micelles is affected by the type, size, and stereochemistry of the surfactant and the solvent environment. And although the concentration of micelles increases as you add more detergent to the solution, the concentration of detergent monomers stays constant above the CMC.
So, how do they solubilize protein membranes? As you may already know, biological membranes have the same amphipathic properties as detergents. They have a charged polar head connected to two hydrophobic tails and form a bilayer (the hydrophobic tails are sandwiched between two faces of polar head groups). Found between these layers are your proteins and lipids.
You cannot release these proteins in aqueous solutions since they are tightly held in the lipid bilayer by the hydrophobic interactions between the lipid tails and hydrophobic protein domains. However, you can extract your target proteins by using the most appropriate detergent solution.
