title: Structure and stability of self-assembled actin-lysozyme complexes in salty water.
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.
authors.affiliation: Department of Materials Science and Engineering, University of Illinois at Urbana-Champaign, 61801, USA.
authors.forename: Lori K
authors.initials: LK
authors.lastname: Sanders
authors.forename: Camilo
authors.initials: C
authors.lastname: Guáqueta
authors.forename: Thomas E
authors.initials: TE
authors.lastname: Angelini
authors.forename: Jae-Wook
authors.initials: JW
authors.lastname: Lee
authors.forename: Scott C
authors.initials: SC
authors.lastname: Slimmer
authors.forename: Erik
authors.initials: E
authors.lastname: Luijten
authors.forename: Gerard C L
authors.initials: GC
authors.lastname: Wong
mesh_terms: D000199:Actins / Q000737:chemistry* / Q000378:metabolism; D009113:Muramidase / Q000737:chemistry* / Q000378:metabolism; D009997:Osmotic Pressure; D012965:Sodium Chloride / Q000737:chemistry; D012996:Solutions; D014867:Water / Q000737:chemistry; D014961:X-Ray Diffraction
chemical_list: D000199:Actins; D012996:Solutions; D014867:Water; D012965:Sodium Chloride; D009113:Muramidase