Structure and Stability of Self-Assembled Actin-Lysozyme Complexes in Salty Water

Journal Article · Fri Sep 02 00:00:00 EDT 2005 · Physical Review Letters

DOI:https://doi.org/10.1103/PhysRevLett.95.108302· OSTI ID:20699402

Sanders, Lori K; Guaqueta, Camilo; Lee, Jae-Wook; Slimmer, Scott C; Luijten, Erik ^[1]; Angelini, Thomas E ^[2]; Wong, Gerard C.L. ^[1]

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1. Department of Materials Science and Engineering, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801 (United States)
2. Department of Physics, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801 (United States)

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.

• OSTI ID: 20699402
• Journal Information: Physical Review Letters, Vol. 95, Issue 10; Other Information: DOI: 10.1103/PhysRevLett.95.108302; (c) 2005 The American Physical Society; Country of input: International Atomic Energy Agency (IAEA); ISSN 0031-9007
• Country of Publication: United States
• Language: English

Related Subjects

71 CLASSICAL AND QUANTUM MECHANICS
GENERAL PHYSICS
ACTIN
BIOPHYSICS
ELECTROLYTES
LYSOZYME
MOLECULAR DYNAMICS METHOD
POLYMERS
SALTS
SIMULATION
SMALL ANGLE SCATTERING
STABILITY
X-RAY DIFFRACTION