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We have analyzed dynamics on the complex free energy landscape of proteinfolding in the FOLD-X model, by calculating for each state of the system themean first passage time to the folded state. The resulting kinetic map of thefolding process shows that it proceeds in jumps between well-defined, localfree energy minima. Closer analysis of the different local minima allows us toreveal secondary, parallel pathways as well as dead ends.Comment: 7 page

Mean first-passage time analysis reveals rate-limiting steps, parallel pathways and dead ends in a simple model of protein folding