abstract:Hydrophobic collapse is a hypothesized event that occurs during the folding process of globular proteins, suggested on the basis of the observation that proteins' native states often contain a hydrophobic core of nonpolar amino acid side chains (interspersed with charged side chains that are neutralized by salt bridges) in the protein's interior, leaving most of the polar or charged residues on the solvent-exposed protein surface. The energetic stabilization conferred on the protein by the sequestration of the hydrophobic side chains from the surrounding water is thought to stabilize folding intermediates.