[Nonlinear elasticity and dynamics of globular proteins]

Abstract

A molecule of native protein exhibits a high degree of mechanical nonlinearity, which gives rise to a peculiar dynamics behavior of globular proteins. Intramolecular motions strongly depend on pressure. The reaction of specific volume to the action of electric field (electrostriction) inside the molecule has a sign opposite to that observed in liquids. The probability that a small ion would penetrate inside the globule from the solvent depends nonmonotonously on hydrostatic pressure. The nonmonotonicity should manifest itself in all processes related to the transfer of ions inside the globule. The relationship between the mechanical properties of the protein and the kinetics of hydrogen exchange at normal and high pressure is discussed.