Journal
PHYSICAL REVIEW E
Volume 67, Issue 5, Pages -Publisher
AMER PHYSICAL SOC
DOI: 10.1103/PhysRevE.67.051404
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The osmotic virial coefficient B-2 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 B-2 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 B-2 is compared with experiments. Implications for protein crystallization are discussed.
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