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. Author manuscript; available in PMC: 2011 Jul 28.
Published in final edited form as: Proteins. 2010 Dec;78(16):3260–3269. doi: 10.1002/prot.22833

Figure 2.

Figure 2

Free energy diagrams of the minimal three-state model for fold switching. Vertical arrows indicate free energy changes; RT and logarithm terms are omitted for clarity. Represented in black are the free energy levels of Q65 and Q65′, in which the stabilities of N and N′ are approximately equal(KfoldN =KfoldN′). Ligand binding to N is shown (e.g., the Q65′ variant). (A) The effect of introducing a destabilizing mutation into N, depicted in gray, is to decrease binding affinity and increase fluorescence change. (B) The effect of introducing a destabilizing mutation into N′, shown in gray, is to decrease the height of the rate-limiting barrier (KunfN′).