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. Author manuscript; available in PMC: 2023 Aug 1.
Published in final edited form as: Biophys Chem. 2022 Apr 29;287:106821. doi: 10.1016/j.bpc.2022.106821

Figure 5. Representative protein folding energy landscapes.

Figure 5.

(A) Folding funnel proposed by Wolynes and coworkers, showing how protein conformational entropy decreases in concert with effective potential energy, as a protein folds to its native state [104, 116]. (B) Helmholtz free energy landscape for proteins that do not have a free-energy transition state for folding. (C) Helmholtz free energy landscape for proteins that have a free-energy transition state for folding. In panels A-C, the native state has 100% native contacts (Q = 1), and the unfolded state has Q = 0. (D) Multidimensional energy landscape. The vertical axis represents the potential energy of any given protein conformation plus the free energy of solvation [113]. Figure 1D is reprinted with permission from John Wiley and Sons [41] from figure 37C in Protein Science 4, Dill, K. A.; Bromberg, S.; Yue, K.; Chan, H. S.; Ftebig, K. M.; Yee, D. P.; Thomas, P. D. Principles of Protein Folding — a Perspective from Simple Exact Models. 4, 561–602. Copyright (1995). (E) Standard-state Gibbs free energy landscape of a protein that cannot form aggregates at a given temperature, pressure and solution conditions. (F) Gibbs free energy landscape for a protein that can form aggregates at a given temperature, pressure and solution conditions.