In a cellular environment, confinement and macromolecular crowding play an important role in thermal stability and folding kinetics of a protein. We have resorted to a generalized version of the Wako-Saitô-Muñoz-Eaton model for protein folding to study the behavior of six different protein structures confined between two walls. Changing the distance 2R between the walls, we found, in accordance with previous studies, two confinement regimes: starting from large R and decreasing R, confinement first enhances the stability of the folded state as long as this is compact and until a given value of R; then a further decrease of R leads to a decrease of folding temperature and folding rate. We found that in the low confinement regime, both unfolding temperatures and logarithm of folding rates scale as R(-γ) where γ values lie in between 1.42 and 2.35.