Interactions between actin, an anionic polyelectrolyte, and lysozyme, a cationic globular protein, have been examined using a combination of synchrotron small-angle x-ray scattering and molecular dynamics simulations. Lysozyme initially bridges pairs of actin filaments, which relax into hexagonally-coordinated columnar complexes comprised of actin held together by incommensurate one-dimensional close-packed arrays of lysozyme macroions. These complexes are found to be stable even in the presence of significant concentrations of monovalent salt, which is quantitatively explained from a redistribution of salt between the condensed and the aqueous phases.
@article{arxiv.cond-mat/0507584,
title = {Structure and stability of self-assembled actin-lysozyme complexes in salty water},
author = {Lori K. Sanders and Camilo Guaqueta and Thomas E. Angelini and Jae-Wook Lee and Scott C. Slimmer and Erik Luijten and Gerard C. L. Wong},
journal= {arXiv preprint arXiv:cond-mat/0507584},
year = {2007}
}