Mechanochemical enzymes and protein machines as hydrodynamic force dipoles: The active dimer model

Abstract

Mechanochemically active enzymes change their shapes within every turnover cycle. Therefore, they induce circulating flows in the solvent around them and behave as oscillating hydrodynamic force dipoles. Because of non-equilibrium fluctuating flows collectively generated by the enzymes, mixing in the solution and diffusion of passive particles within it are expected to get enhanced. Here, we investigate the intensity and statistical properties of such force dipoles in the minimal active dimer model of a mechanochemical enzyme. In the framework of this model, novel estimates for hydrodynamic collective effects in solution and in lipid bilayers under rapid rotational diffusion are derived, and available experimental and computational data is examined.

arXiv comment16 pages, 7 figures

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Cited by in corpus (12)

• Non-reciprocal response of a two-dimensional fluid with odd viscosity
• Hydrodynamic lift of a two-dimensional liquid domain with odd viscosity
• Time-correlation functions for odd Langevin systems
• Nonequilibrium Transport Induced by Biological Nanomachines
• Hydrodynamics of an odd active surfer in a chiral fluid
• Synchronization and enhanced catalysis of mechanically coupled enzymes
• Pair dynamics of active force dipoles in an odd-viscous fluid
• Collective synchronization of dissipatively-coupled noise-activated processes
• Odd elasticity of a catalytic micromachine
• Interplay between Brownian and hydrodynamic tracer diffusion in suspensions of swimming microorganisms
• Reaction-induced molecular dancing and boosted diffusion of enzymes
• Dumbbell dimer dynamics in three-dimensional chiral fluids