Protein Stability
For the unfolding reaction of Protein G, ΔH° =210.6 kJ/mol, this means that

unfolding is favored enthalpically
folding is favored enthalpically
the entropy is negative at all temperatures
the entropy is positive at all temperatures

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Protein Stability
The correlation between free energy ΔG transfer between the aqueous/organic phases and the surface area of amino acid residues

is only meaningful for the polar amino acids
ignores the important contribution of the peptide bond
is similar to effects seen with SDS denaturation
reflects the reduction in solvent-accessible area during protein folding

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