Nonequilibrium self-assembly of multiple stored targets in a dimer-based system
Abstract
Nonequilibrium self-assembly can be found in various biological processes where chemical potential gradients are exploited to steer the system to a desired organized structure with a particular function. Microtubules, for example, are composed of two globular protein subunits, α-tubulin and β-tubulin, which bind together to form polar dimers that self-assemble a hollow cylinder structure in a process driven by GTPase activity. Inspired by this process, we define a generic self-assembly lattice model containing particles of two subunits, which is driven out-of-equilibrium by a dimer-favoring local driving force. Using Monte Carlo simulations, we characterize the ability of this system to restore pre-encoded target structures as a function of the initial seed size, interaction energy, chemical potential, number of target structures, and strength of the nonequilibrium drive. We demonstrate some intriguing consequences of the drive, such as a smaller critical seed and an improved target assembly stability, compared to the equilibrium scenario. Our results can expand the theoretical basis of nonequilibrium self-assembly and provide deeper understanding of how nonequilibrium driving can overcome equilibrium constraints.
Document Details
- Document Type
- Pub Defense Publication
- Publication Date
- Dec 20, 2021
- Source ID
- 10.1063/5.0069161
Entities
People
- Adi Ben-Ari
- Gili Bisker
- Liron Ben-Ari
Organizations
- Air Force Office of Scientific Research
- Army Research Office
- Israel Science Foundation
- Ministry of Science and Technology, Israel
- Tel Aviv University