  A transfer-matrix formalism is introduced to evaluate exactly the partition
function of the Munoz-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 as a first tool to
characterize the dynamics of a protein of known native state and equilibrium
population. Applications to a $\beta$-hairpin and to protein CI-2, with
comparisons to previous results, are also shown.
