  We study the thermodynamical properties of a topology-based model proposed by
Galzitskaya and Finkelstein for the description of protein folding. We devise
and test three different mean-field approaches for the model, that simplify the
treatment without spoiling the description. The validity of the model and its
mean-field approximations is checked by applying them to the $\beta$-hairpin
fragment of the immunoglobulin-binding protein (GB1) and making a comparison
with available experimental data and simulation results. Our results indicate
that this model is a rather simple and reasonably good tool for interpreting
folding experimental data, provided the parameters of the model are carefully
chosen. The mean-field approaches substantially recover all the relevant exact
results and represent reliable alternatives to the Monte Carlo simulations.
