Protein Denaturation Induced by Pressure Studied by Molecular Dynamics Simulation

C. GASTÓN FERRARA; J. RAÚL GRIGERA; MCCARTHY, A.N

New Mexico

Congreso; Meeting: Protein under Pressure; 2008

CNLS

We have analized the effect of pressure on the denaturation of proteins bt molecular dynamics simulations. Due to the time response of proteins to pressure, relatively long simulations are required. Lysozyme and Apomyoglobin, two limiting cases of the behavior of globular proteins under pressure, were selected for the study. The results obteined for Lysozymecoincide both with the experimental observations and with the generally established idea that high-pressure classical molecular dynamic simulations only produce elastic changes around the native conformer. On the contrary, in the case of Apomyoglobin a total disruption of the native structure is observed, secundary to the increase in hydrophobic and total solvent accessed surface (SAS). We attribute the denaturing action of pressure mainly to its effect on water properties.