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

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

2003-03-28

arxiv.org/abs/cond-mat/0303604v1

Europhysics Letters 61, 561-566 (2003)

Physics

Condensed Matter

Statistical Mechanics

7 pages

Scientific paper

10.1209/epl/i2003-00165-4

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

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