%0 Journal Article
%J Physical Biology
%D 2012
%T Effects of confinement on thermal stability and folding kinetics in a simple Ising-like model
%A M Caraglio
%A Pelizzola, A
%K biocomp
%K statphys
%P 016006
%U http://stacks.iop.org/1478-3975/9/i=1/a=016006
%V 9
%X 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 2 R 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.