what is the driving force for protein folding in aqueous solvent?
Answer: Hydrophobic strength is a significant driving force behind protein folding. The polar side chains are usually directed and interact with water, while the hydrophobic center of the folded protein consists of non-polar side chains.
The hydrophobic effect is known to be the main driving force for the folding of globular proteins. The effect is the burying of the hydrophobic residues in the protein core. It is exemplified by the fact that oil and water are not mixed together.