Packing defects and the width of biopolymer bundles
arXiv:0708.3903 · doi:10.1103/PhysRevE.78.011916
Abstract
The formation of bundles composed of actin filaments and cross-linking proteins is an essential process in the maintenance of the cells' cytoskeleton. It has also been recreated by in-vitro experiments, where actin networks are routinely produced to mimic and study the cellular structures. It has long been observed that these bundles seem to have a well defined width distribution, which has not been adequately described theoretically. We propose here that packing defects of the filaments, quenched and random, contribute an effective repulsion that counters the cross-linking adhesion energy and leads to a well defined bundle width. This is a two-dimensional strain-field version of the classic Rayleigh instability of charged droplets.
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Cited by in corpus (10)
- Cooperativity and Frustration in Protein-Mediated Parallel Actin Bundles
- Statics and Dynamics of the Wormlike Bundle Model
- Braided Bundles and Compact Coils: The Structure and Thermodynamics of Hexagonally-Packed, Chiral Filament Assemblies
- Stall force of polymerizing microtubules and filament bundles
- Zipping mechanism for force-generation by growing filament bundles
- Theory of Crosslinked Bundles of Helical Filaments: Intrinsic Torques in Self-Limiting Biopolymer Assemblies
- Bundle formation in parallel aligned polymers with competing interactions
- Depletion-Driven Morphological Control of Bundled Actin Networks
- Defect-driven shape instabilities of bundles
- Monodisperse domains by proteolytic control of the coarsening instability