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The Effect of Hydrostatic Pressure on Protein Crystals Investigated by Molecular Simulation

  • Darrin M. York
  • Tom A. Darden
  • Lee G. Pedersen
Conference paper
Part of the The Jerusalem Symposia on Quantum Chemistry and Biochemistry book series (JSQC, volume 27)

Abstract

The effect of hydrostatic pressure on protein crystal structures is examined with molecular simulation. Four 1 ns molecular dynamics simulations of bovine pancreatic trypsin inhibitor in a crystal unit cell have been performed at solvent densities corresponding to 32%, 36%, 40%, and 44% solvent. Electrostatic interactions in the crystalline environment were treated rigorously with Ewald sums. The effect of varying the solvent density at constant unit cell volume is analyzed with respect to changes in protein structure, atomic fluctuations, solvation, and crystal packing. The results indicate the solvent density range 36–40% gives excellent overall agreement with high resolution crystallographic data (~O.3Å rms backbone deviation). The low density (32%) and high density (44%) simulations have larger deviations.

Key words

Crystal Ewald molecular dynamics pressure protein simulation 

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Copyright information

© Springer Science+Business Media Dordrecht 1995

Authors and Affiliations

  • Darrin M. York
    • 1
    • 2
  • Tom A. Darden
    • 4
  • Lee G. Pedersen
    • 3
    • 4
  1. 1.Department of ChemistryDuke UniversityDurhamUSA
  2. 2.a Division of MCNCNorth Carolina Supercomputing CenterRTPUSA
  3. 3.Department of ChemistryUniversity of North CarolinaChapel HillUSA
  4. 4.National Institute of Environmental Health SciencesResearch Triangle ParkUSA

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