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Contributions to the free energy of folding of globular proteins

Contributions to the free energy of folding of globular proteins
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Description: The conformational entropy change works against folding, but the enthalpy of internal interactions and the entropy change from the hydrophobic effect favor folding.

Summing these three quantities makes the total free energy of folding negative (favorable); thus, the folded structure is stable.

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Source: https://biology-forums.com/index.php?action=gallery;sa=view;id=34098
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