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 α- and γ-positions are slightly decreased at 5000 atm. The mobility of the backbone φ-and ψ-angles...

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Bibliographic Details
Published in:FEBS letters 1993-06, Vol.323 (3), p.215-217
Main Authors: Brunne, R.M., van Gunsteren, W.F.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Analytical, structural and metabolic biochemistry
Animals
Aprotinin - chemistry
Biological and medical sciences
BPTI
BPTI, bovine pancreatic trypsin inhibitor
Cattle
Computer simulation
Enzymes and enzyme inhibitors
Fundamental and applied biological sciences. Psychology
Hydrolases
Hydrostatic pressure
MD, molecular dynamics
Molecular dynamics
NMR, nuclear magnetic resonance
Pressure
Protein Conformation
RMS, root mean square
X-Ray Diffraction
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Summary: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.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(93)81342-W