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The Energy Landscapes of Repeat-Containing Proteins: Topology, Cooperativity, and the Folding Funnels of One-Dimensional Architectures

Figure 2

Numerical calculations of the analytical model for a finite protein of N = 14 undergoing thermal denaturation.

(A) Fraction folded as a function of temperature (T) at increasing εSi = 0.5, α = 2, s0 = 8 fixed)(black solid lines), increasing εiS = 2.5, s0 = 8 fixed) (gray lines) and decreasing s0S = 2.5, εi = 0.5 fixed) (black dashed lines). (B) Dependence of the transition temperature between the fully folded and the fully unfolded states (Tf) for the changes in parameters described in (A). Insert: cooperativity of the folding transition as a function of the varied parameters. (B) Relationship between Tf and m-values for changes in parameters described in (A).

Figure 2

doi: https://doi.org/10.1371/journal.pcbi.1000070.g002