2005/07/25 by Lori K. Sanders, Camilo Guáqueta, Camilo Guaqueta +5
Chemistry · Materials Science · Physics and Astronomy · #Electrostatics and Colloid Interactions #Material Dynamics and Properties #Polymer Surface Interaction Studies #cond-mat.soft #physics.bio-ph
paper · pdf · doi:10.1103/physrevlett.95.108302
published as Phys. Rev. Lett. 95, 108302 (2005) · Accepted for publication in Phys. Rev. Lett
arxiv created 2005/07/25 · openalex publication_date 2005/09/01 · arxiv updated 2009/12/01 · openalex created_date 2025/10/10 · openalex updated_date 2026/07/28
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.