The stability of the folded structure of a globular protein depends on the interplay of which of these factors:
1)ΔH generally favors the folded state and is associated with changes in noncovalent bonding interactions.
2)ΔH of the surrounding medium, which generally favors the folded state of the protein.
3)ΔSconformation of the protein favors the unfolded state.
4)ΔSsolvent is favorable due to the release of water from clathrates. This occurs when solvent exposed hydrophobic groups become buried within the molecule.