Dynamical properties of bovine pancreatic trypsin inhibitor from a molecular dynamics simulation at 5000 atm

Abstract

Molecular dynamics simulations of bovine pancreatic trypsin inhibitor in water have been performed with coupling to pressure baths at 1 atm and at 5000 atm. The positional fluctuations of atoms in the α- and γ-positions are slightly decreased at 5000 atm. The mobility of the backbone φ-and ψ-angles is not affected with respect to the root mean square fluctuations and the rate of torsional angle transitions. The amplitude of libration of sidechain χ-angles remains nearly the same for both pressures, but the rate of torsional angle transitions decreases on average by 30% when increasing the hydrostatic pressure to 5000 atm