Dynamical properties of bovine pancreatic trypsin inhibitor from a molecular dynamics simulation at 5000 atm.
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 alpha- and gamma-positions are slightly decreased at 5000 atm. The mobility of the backbone phi- and psi-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 chi-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.
Brunne
R M
RM
Laboratorium für Physikalische Chemie, Eidgenössische Technische Hochschule, ETH Zentrum, Zürich, Switzerland.
van Gunsteren
W F
WF
D000595:Amino Acid Sequence; D000818:Animals; D007611:Aprotinin / Q000737:chemistry*; D002417:Cattle; D011312:Pressure; D011487:Protein Conformation; D014961:X-Ray Diffraction
D007611:Aprotinin