Nonmonotonic variation with salt concentration of the second virial coefficient in protein solutions

E. Allahyarov, H. Löwen, J. P. Hansen, and A. A. Louis
Phys. Rev. E 67, 051404 – Published 16 May 2003
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Abstract

The osmotic virial coefficient B2 of globular protein solutions is calculated as a function of added salt concentration at fixed pH by computer simulations of the “primitive model.” The salt and counterions as well as a discrete charge pattern on the protein surface are explicitly incorporated. For parameters roughly corresponding to lysozyme, we find that B2 first decreases with added salt concentration up to a threshold concentration, then increases to a maximum, and then decreases again upon further raising the ionic strength. Our studies demonstrate that the existence of a discrete charge pattern on the protein surface profoundly influences the effective interactions and that linear and nonlinear Poisson Boltzmann theories fail for large ionic strength. The observed nonmonotonicity of B2 is compared with experiments. Implications for protein crystallization are discussed.

  • Received 21 February 2003

DOI:https://doi.org/10.1103/PhysRevE.67.051404

©2003 American Physical Society

Authors & Affiliations

E. Allahyarov1, H. Löwen2, J. P. Hansen3, and A. A. Louis3

  • 1Institut für Festkörperforschung, Forschungszentrum Jülich, D-52425 Jülich, Germany
  • 2Institut für Theoretische Physik II, Heinrich-Heine-Universität Düsseldorf, D-40225 Düsseldorf, Germany
  • 3Department of Chemistry, Lensfield Road, Cambridge CB2 1EW, United Kingdom

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Vol. 67, Iss. 5 — May 2003

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