Figure 2.

The relationship between protein unfolding and internal energy (the data were extracted from [21,38]). (A) Shows the possible quantities of ΔG_unfolding at different temperatures. (B) Indicates the several stages of the protein unfolding pathway. At first, by obtaining energy, the protein is activated to higher levels by increasing the amount of internal energy, and at a critical point, it unfolds by releasing energy to reach a more stable state. In a large number of studies, it is believed that the most stable state of a protein is its aggregated form (fibril form), however, some researchers believe that its natural form is the most stable state.