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

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dc.creatorSanders, Lori K.
dc.creatorGuaqueta, Camilo
dc.creatorAngelini, Thomas E.
dc.creatorLee, Jae-Wook
dc.creatorSlimmer, Scott C.
dc.creatorLuijten, Erik
dc.creatorWong, Gerard C. L.
dc.date2005-07-25
dc.date.accessioned2026-07-07T03:06:06Z
dc.date.available2026-07-07T03:06:06Z
dc.descriptionInteractions 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.
dc.descriptionAccepted for publication in Phys. Rev. Lett
dc.identifierhttps://arxiv.org/abs/cond-mat/0507584
dc.identifierhttp://arxiv.org/abs/cond-mat/0507584
dc.identifierPhys. Rev. Lett. 95, 108302 (2005)
dc.identifierdoi:10.1103/PhysRevLett.95.108302
dc.identifier.urihttp://salesiana.dossiersoluciones.com/handle/123456789/26692
dc.subjectSoft Condensed Matter
dc.subjectBiological Physics
dc.titleStructure and stability of self-assembled actin-lysozyme complexes in salty water
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