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

FEBS Letters

Brunne, R.M.¹  van Gunsteren, W.F.¹ 

[1] Laboratorium für Physikalische Chemie, Eidgenössische Technische Hochschule, ETH Zentrum, CH-8092 Zürich, Switzerland

关键词: BPTI;    Molecular dynamics;    Hydrostatic pressure;    Computer simulation;    BPTI;    bovine pancreatic trypsin inhibitor;    MD;    molecular dynamics;    NMR;    nuclear magnetic resonance;    RMS;    root mean square;   

DOI  :  10.1016/0014-5793(93)81342-W

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown