What mechanism do detergents use to solubilize membrane proteins?

Detergents play a crucial role in solubilizing membrane proteins through the formation of micelles, which effectively surround the hydrophobic regions of these proteins. Membrane proteins are typically embedded within lipid bilayers, presenting a challenge to isolate and study them. Detergents are amphipathic molecules, meaning they have both hydrophilic (water-attracting) and hydrophobic (water-repelling) parts.

When detergents are introduced, their hydrophobic tails interact with the hydrophobic regions of the membrane proteins, while the hydrophilic heads remain in contact with the surrounding aqueous environment. This interaction leads to the formation of micelles, which encapsulate the protein, allowing it to be suspended in solution without aggregating or precipitating out. This solubilization is essential for various biochemical techniques, such as purification and functional assays of membrane proteins.

The other mechanisms listed, such as dissociating proteins from nucleic acids, degrading proteins chemically, or inducing thermal denaturation, do not accurately describe the primary function of detergents in this context. Instead, they may refer to other processes that are not directly involved in the solubilization of membrane proteins.