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Hydrophobic Interaction
Linked via "amyloidoses"
Protein Folding
In globular proteins, the hydrophobic interaction is the primary driving force behind the collapse of the polypeptide chain into its native conformation. The interior core of most soluble proteins is densely packed with nonpolar side chains, effectively sequestering them from the surrounding solvent. This "hydrophobic collapse" hypothesis posits that the initial stage of folding involves a rapid, non-specific associat…