Which process determines stability of a protein folded based on hydrophobic interactions described by free energy functions?

💡 Explanation

When a protein folds, minimization of total free energy dictates that the protein will adopt the conformation that results in the lowest energy state overall, arising primarly from driving hydrophobic amino acids into the molecule's core. Therefore minimization of total energy leads to overall protein stability, rather than just optimizing surface hydrophobicity, H-bonds or eletrostatics alone.

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