Given that the surroundings' net ΔS is positive and the process as a whole has a negative G, this entropic cost does not stop spontaneous protein folding.
Description of the protein folding and entropy penalty scenario:
- The decrease in the solvation zone is linked to a considerable gain in positive entropy, which compensates for the entropic penalty brought on by the greater organization in the protein folding condition. The hydrophobic effect is another name for this phenomenon. The operation remains spontaneous as a result of allowing the net Gibbs free energy shift should become minus.
- Due to the lack of stabilizing connections, an unfolded protein has a high configurational entropy as well as a high enthalpy. The entropy and enthalpy of a folded protein are greatly reduced. Here, there is a compromise between H and S. The S component is weighted more heavily by increased temperature because ΔG = ΔH - TΔ S, which means that unfolding is favored by greater temperature.
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