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A Consistent Experimental and Modeling Approach to Light-Scattering Studies of Protein-Protein Interactions in Solution

D. Asthagiri ^*, A. Paliwal , D. Abras , A. M. Lenhoff  and M. E. Paulaitis 

^* Theoretical Division, Los Alamos National Laboratory, Los Alamos, New Mexico 87544; Department of Chemical and Biomolecular Engineering, Johns Hopkins University, Baltimore, Maryland 21218; and Department of Chemical Engineering, University of Delaware, Newark, Delaware 19716

Correspondence: Address reprint requests to M. E. Paulaitis, E-mail: paulaitis.1{at}osu.edu.

The osmotic second virial coefficient, B₂, obtained by light scattering from protein solutions has two principal components: the Donnan contribution and a contribution due to protein-protein interactions in the limit of infinite dilution. The Donnan contribution accounts for electroneutrality in a multicomponent solution of (poly)electrolytes. The importance of distinguishing this ideal contribution to B₂ is emphasized, thereby allowing us to model the interaction part of B₂ by molecular computations. The model for protein-protein interactions that we use here extends earlier work (Neal et al., 1998) by accounting for long-range electrostatic interactions and the specific hydration of the protein by strongly associated water molecules. Our model predictions are compared with measurements of B₂ for lysozyme at 25°C over pH from 5.0 to 9.0, and 7–60 mM ionic strength. We find that B₂ is positive at all solution conditions and decreases with increasing ionic strength, as expected, whereas the interaction part of B₂ is negative at all conditions and becomes progressively less negative with increasing ionic strength. Although long-range electrostatic interactions dominate this contribution, particularly at low ionic strength, short-range electrostatic/dispersion interactions with specific hydration are essential for an accurate description of B₂ derived from experiment.

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