European Biophysics Journal

, Volume 24, Issue 3, pp 137–141 | Cite as

Orientational steering in enzyme-substrate association: Ionic strength dependence of hydrodynamic torque effects

  • Jan Antosiewicz
  • James M. Briggs
  • J. Andrew McCammon
Article

Abstract

The effect of hydrodynamic torques on the association rate constants for enzyme-ligand complexation is investigated by Brownian dynamics simulations. Our hydrodynamic models of the enzyme and ligand are composed of spherical elements with friction forces acting at their centers. A quantitative measure of hydrodynamic torque orientational effects is introduced by choosing, as a reference system, an enzyme-ligand model with the same average hydrodynamic interactions but without orientational dependence. Our simple models show a 15% increase in the rate constant caused by hydrodynamic torques at physiological ionic strength. For more realistic hydrodynamic models, which are not computationally feasible at present, this effect is probably higher. The most important finding of this work is that hydrodynamic complementarity in shape (i.e. like the fitting together of pieces of a puzzle) is most effective for interactions between molecules at physiological ionic strength.

Key words

Hydrodynamic torques Enzyme-substrate association Ionic strength dependence 

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Copyright information

© Springer-Verlag 1996

Authors and Affiliations

  • Jan Antosiewicz
    • 1
    • 2
  • James M. Briggs
    • 1
    • 2
  • J. Andrew McCammon
    • 1
    • 2
  1. 1.Department of Chemistry and BiochemistryUniversity of California at San DiegoLa JollaUSA
  2. 2.Department of PharmacologyUniversity of California at San DiegoLa JollaUSA
  3. 3.Department of BiophysicsUniversity of WarsawWarsawPoland

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