Alessandro Pelizzola

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The cluster variation method (CVM) is a hierarchy of approximate variational techniques for discrete (Ising–like) models in equilibrium statistical mechanics, improving on the mean–field approximation and the Bethe–Peierls approximation, which can be regarded as the lowest level of the CVM. In recent years it has been applied both in statistical physics and(More)
Terminal respiratory failure was reversed in three patients with a combination of extra-corporeal CO2 removal through a membrane lung and oxygen diffusion into the diseased lungs between mechanical breaths induced at a frequency of 2-3/min. The technique seems to prevent the pulmonary barotrauma and extrapulmonary derangements caused by conventional(More)
A transfer-matrix formalism is introduced to evaluate exactly the partition function of the Muñoz-Eaton model, relating the folding kinetics of proteins of known structure to their thermodynamics and topology. This technique can be used for a generic protein, for any choice of the energy and entropy parameters, and in principle allows the model to be used(More)
Mechanical unfolding and refolding of ubiquitin are studied by Monte Carlo simulations of a Gō model with binary variables. The exponential dependence of the time constants on the force is verified, and folding and unfolding lengths are computed, with good agreement with experimental results. Furthermore, the model exhibits intermediate kinetic states, as(More)
Exactness of the cluster variation method and factorization of the equilibrium probability for the Wako–Saitô–Muñoz–Eaton model of protein folding Abstract. I study the properties of the equilibrium probability distribution of a protein folding model originally introduced by Wako and Saitô, and later reconsidered by Muñoz and Eaton. The model is a(More)
A simple model, recently introduced as a generalization of the Wako-Saito; model of protein folding, is used to investigate the properties of widely studied molecules under external forces. The equilibrium properties of the model proteins, together with their energy landscape, are studied on the basis of the exact solution of the model. Afterwards, the(More)
Previous research has shown a strong correlation of protein folding rates to the native state geometry, yet a complete explanation for this dependence is still lacking. Here we study the rate-geometry relationship with a simple statistical physics model, and focus on two classes of model geometries, representing ideal parallel and antiparallel structures.(More)
The authors address the problem of downhill protein folding in the framework of a simple statistical mechanical model, which allows an exact solution for the equilibrium and a semianalytical treatment of the kinetics. Focusing on protein 1BBL, a candidate for downhill folding behavior, and comparing it to the WW domain of protein PIN1, a two-state folder of(More)