Behavior of Proteins under Pressure from Experimental Pressure-Dependent Structures

Structure-based models are coarse-grained representations of the interactions responsible for protein folding process. In their simplest form, they use only native contact map a given to predict main features its process by computer simulation. Given limitations, these frequently complemented with sequence-dependent contributions or additional information. Specifically, analyze effect pressure on folding/unfolding transition, special forms interaction potentials employed, which may priori determine outcome simulations. this work, we have tried keep original simplicity structure-based models. Therefore, used folded structures that been experimentally determined at different pressures define maps and thus dependent pressure. Despite apparently tiny structural differences induced pressure, our simulation results provide thermodynamic kinetic behaviors, roughly correspond experimental observations (when there is possible comparison) two proteins as benchmarks, hen egg-white lysozyme dihydrofolate reductase. work shows feasibility using global effects physical property