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Abstract
We have applied a simple statistical mechanics Gō-like model to the analysis of the PIN1 WW domain, resorting to mean field and Monte Carlo techniques to characterize its thermodynamics, and comparing the results with the wealth of available experimental data. PIN1 WW domain is a 39-residue protein fragment which folds on an antiparallel β-sheet, thus representing an interesting model system to study the behavior of these secondary structure elements. Results show that the model correctly reproduces the two-state behavior of the protein, and also the trends of the experimental ϕ T values. Moreover, there is a good agreement between Monte Carlo results and the mean field ones, which can be obtained with a substantially smaller computational effort.
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