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| - A Minimal Model of Three-State Folding Dynamics of Helical Proteins
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| - A diffusion-collision-like model is proposed for helical proteins with three-state folding dynamics. The modelgeneralizes a previous scheme based on the dynamics of putatively essential parts of the protein (foldons)that was successfully tested on proteins with two-state folding. We show that the extended model, unlike theoriginal one, allows satisfactory calculation of the folding rate and reconstruction of the salient steps of thefolding pathway of two proteins with three-state folding (Im7 and p16). The dramatic reduction of variablesachieved by focusing on the foldons makes our model a good candidate for a minimal description of thefolding process also for three-state folders. Finally, the applicability of the foldon diffusion-collision modelto two-state and three-state folders suggests that different folding mechanisms are amenable to conceptuallyhomogeneous descriptions. The implications for a unification of the variety of folding theories so far proposedfor helical proteins are discussed in the final discussion.
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