Structure and stability of self-assembled actin-lysozyme complexes in salty water.
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.
Sanders
Lori K
LK
Department of Materials Science and Engineering, University of Illinois at Urbana-Champaign, 61801, USA.
Guáqueta
Camilo
C
Angelini
Thomas E
TE
Lee
Jae-Wook
JW
Slimmer
Scott C
SC
Luijten
Erik
E
Wong
Gerard C L
GC
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
D000199:Actins; D012996:Solutions; D014867:Water; D012965:Sodium Chloride; D009113:Muramidase