Ionic detergents are commonly used to solubilize membrane proteins due to their ability to dissociate lipids and stabilize proteins. When added to a solution containing membrane proteins, the polar heads of the detergent interact with water, while the hydrophobic chains insert themselves into the lipid bilayer, surrounding the membrane proteins. This separates the proteins from the membrane and solubilizes them in the solution.

Ionic detergents also stabilize membrane proteins by preventing their aggregation and denaturation. The detergent's polar heads form electrostatic interactions with the charges present on the proteins, helping to maintain their structure and function.

It is crucial to choose the right ionic detergent based on the specific properties of the membrane proteins. Different detergents have different affinities for proteins and can influence their stability and activity.

Detergents act by disintegrating the lipid bilayer while incorporating lipids and proteins in detergent micelles. The hydrophobic surface areas of the membrane proteins and the lipid "tails" are buried in the hydrophobic interior of the detergent micellar structures, while hydrophilic parts of the proteins are in contact with the aqueous environment.

In protein research, detergents are used to lyse cells, release soluble proteins, solubilize membrane proteins and lipids, control protein crystallization, and prevent non-specific binding in purification and immunoassay procedures.

Ionic detergents, such as sodium dodecyl sulfate (SDS), are extremely effective in the solubilization of membrane proteins but are almost always denaturing to the proteins