Structure and stability of self-assembled actin-lysozyme complexes in salty water

Lori K. Sanders*, Camilo Guáqueta, Thomas E. Angelini, Jae Wook Lee, Scott C. Slimmer, Erik Luijten, Gerard C L Wong

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

39 Scopus citations


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 languageEnglish (US)
Article number108302
JournalPhysical review letters
Issue number10
StatePublished - Sep 2 2005

ASJC Scopus subject areas

  • Physics and Astronomy(all)


Dive into the research topics of 'Structure and stability of self-assembled actin-lysozyme complexes in salty water'. Together they form a unique fingerprint.

Cite this