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We investigate protein-protein interactions in solution by small-angle X-rayscattering (SAXS) and theoretical modeling. The structure factor for solutionsof bovine pancreatic trypsin inhibitor (BPTI), myoglobin (Mb), and intestinalfatty acid-binding protein (IFABP) is determined from SAXS measurements atmultiple concentrations, from Monte Carlo simulations with a coarse-grainedstructure-based interaction model, and from analytic approximate solutions oftwo idealized colloidal interaction models without adjustable parameters. Bycombining these approaches, we find that the structure factor is essentiallydetermined by hard-core and screened electrostatic interactions. Other softshort-ranged interactions (van der Waals and solvation-related) are eitherindividually insignificant or tend to cancel out. The structure factor is alsonot significantly affected by charge fluctuations. For Mb and IFABP, with smallnet charge and relatively symmetric charge distribution, the structure factoris well described by a hard-sphere model. For BPTI, with larger net charge,screened electrostatic repulsion is also important, but the asymmetry of thecharge distribution reduces the repulsion from that predicted by a chargedhard-sphere model with the same net charge. Such charge asymmetry may alsoamplify the effect of shape asymmetry on the protein-protein potential of meanforce.

Weak self-interactions of globular proteins studied by small-angle X-ray scattering and structure-based modeling