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Statics, metastable states and barriers in protein folding: A replica variational approach

Shoji Takada·Peter G. Wolynes
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Abstract

Protein folding is analyzed using a replica variational formalism to investigate some free energy landscape characteristics relevant for dynamics. A random contact interaction model that satisfies the minimum frustration principle is used to describe the coil-globule transition (characterized by T_CG), glass transitions (by T_A and T_K) and folding transition (by T_F). Trapping on the free energy landscape is characterized by two characteristic temperatures, one dynamic, T_A the other static, T_K (T_A> T_K), which are similar to those found in mean field theories of the Potts glass. 1)Above T_A, the free energy landscape is monotonous and polymer is melted both dynamically and statically. 2)Between T_A and T_K, the melted phase is still dominant thermodynamically, but frozen metastable states, exponentially large in number, appear. 3)A few lowest minima become thermodynamically dominant below T_K, where the polymer is totally frozen. In the temperature range between T_A and T_K, barriers between metastable states are shown to grow with decreasing temperature suggesting super-Arrhenius behavior in a sufficiently large system. Due to evolutionary constraints on fast folding, the folding temperature T_F is expected to be higher than T_K, but may or may not be higher than T_A. Diverse scenarios of the folding kinetics are discussed based on phase diagrams that take into account the dynamical transition, as well as the static ones.

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Shoji Takada, Peter G. Wolynes. 1997-01-22. Statics, metastable states and barriers in protein folding: A replica variational approach. https://doi.org/10.1103/physreve.55.4562

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