Abstract
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.
Original language | English (US) |
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Article number | 108302 |
Journal | Physical review letters |
Volume | 95 |
Issue number | 10 |
DOIs | |
State | Published - Sep 2 2005 |
ASJC Scopus subject areas
- Physics and Astronomy(all)