The complexation of globular proteins with flexible polyelectrolytes with homogeneous, oppositely charged spheres was discussed using Monte Carlo simulations. The proteins were considered at their respective isoelectric points. A coarse-grained model of the protein shape was also considered in order to take into account the protein excluded volume. A simple statistical analysis of the surface charge density was found sufficient for identifying potential polyelectrolyte binding regions. The protein-only approach identified only possible regions of polyelectrolyte binding, and did not account for any of the polyelectrolyte properties tha influenced binding.
- polyelectrolyte-macroion complexation
- continuous capillary-electrophoresis
- heterogeneously charged surfaces
- bovine serum-albumin
- chain flexibility
- opposite charge