  In cellular environment, confinement and macromulecular crowding play an
important role on thermal stability and folding kinetics of a protein. We have
resorted to a generalized version of the Wako-Saito-Munoz-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-{\gamma} where {\gamma} values lie in
between 1.42 and 2.35.
