Final answer:
Detergents can substitute for lipids in stabilizing integral proteins in aqueous solutions and are particularly effective in hard water due to their amphiphilic nature and more soluble ionic groups.
Step-by-step explanation:
Detergents can substitute for lipids in stabilizing integral proteins while rendering them soluble in aqueous solution. Detergents, like soaps, are amphiphilic, meaning they have both hydrophilic (polar) and hydrophobic (non-polar) parts. This dual nature allows them to interact with the hydrophobic regions of proteins, thus maintaining their solubility in water. Detergents form micelles, which are aggregates where hydrophobic tails are in the interior, protecting them from water, while hydrophilic heads interact with the aqueous environment.
These characteristics make detergents effective in environments with hard water where soaps are less effective due to their tendency to form insoluble compounds with calcium and magnesium. The ionic group in detergents, such as sulfates or sulfonates, is more soluble in hard water, which gives them an advantage over soaps. Moreover, detergents contain synthetic surfactant molecules that can effectively stabilize proteins by forming a protective layer around them.