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

Source: [Rigorous results on the local equilibrium kinetics of a protein folding model](<https://www.sota2.com/research/paper/68fa20a97a2b558e293327ab>)

Collection index: [llms.txt](<https://www.sota2.com/research/llms.txt>)

Data updated: 2025-10-23T22:44:39.259Z

Authors: Marco Zamparo, Alessandro Pelizzola

Published: 2006-07-05T13:44:38.000Z

## 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.

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## Original sources and implementation

[Original paper](<https://arxiv.org/abs/cond-mat/0607118>)

[PDF](<https://arxiv.org/pdf/cond-mat/0607118.pdf>)