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. Author manuscript; available in PMC: 2024 Dec 5.
Published in final edited form as: Curr Opin Chem Biol. 2021 Mar 31;62:90–100. doi: 10.1016/j.cbpa.2021.02.009

Figure 1.

Figure 1

Generic free energy landscape of an intrinsically disordered protein with a propensity to condensate where the free energy of a protein molecule (G) is represented as a function of its degree of structuration (s) and multimerization (n). The letters represent the different minima that may be populated by such molecule, that are illustrated by representative conformations and include highly disordered state (D), partially and fully structures states (PS, FS), an oligomeric state (O), a biomolecular condensate (BC), a hydrogel (HG) and a fibril (F). Changes in the free energy of any state caused by interaction with a small molecule can lead to population shifts or changes in kinetic stability that can be used to alter the propensity of the protein to interact with a binding partner, form condensates or form fibrillar aggregates as shown in Figure 2.