Rigorous results on the local equilibrium kinetics of a protein folding model

Abstract

A local equilibrium approach for the kinetics of a simplified protein folding model, whose equilibrium thermodynamics is exactly solvable, was developed in [M. Zamparo and A. Pelizzola, Phys. Rev. Lett. 97, 068106 (2006)]. Important properties of this approach are (i) the free energy decreases with time, (ii) the exact equilibrium is recovered in the infinite time limit, (iii) the equilibration rate is an upper bound of the exact one and (iv) computational complexity is polynomial in the number of variables. Moreover, (v) this method is equivalent to another approximate approach to the kinetics: the path probability method. In this paper we give detailed rigorous proofs for the above results.

25 pages, RevTeX 4, to be published in JSTAT

References in corpus (2)

• Kinetics of the Wako-Saito-Munoz-Eaton Model of Protein Folding
• Cluster approximations for probabilistic systems: a new perspective of epidemiological modelling

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