We will present results using coarse grained models for two proteins, a three-helix bundle (prb7_53) and protein G, as a function of the geometry and size of the confining potential. From long equilibrium simulations (~ 15 microseconds each) over a range of temperatures, we characterize the thermodynamics and kinetics of folding at each confinement condition and in the bulk. Remarkably, we find that the effect of confinement on folding thermodynamics (stabilization of folded state) for both the proteins closely follows the scaling behavior expected from polymer physics, because the dominant effect of confinement is on the unfolded state which behaves like a random excluded volume chain. We also find that the acceleration in folding kinetics obeys a similar scaling, although small deviations are observed, mainly resulting from transition state confinement. A secondary effect on protein dynamics is the confinement-induced change in local diffusion coefficients, most notably near the unfolded state basin. However, we do not find any net slowdown in the folding rate even for very small confining cavities.