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

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Mikhailov,  Alexander S.
Physical Chemistry, Fritz Haber Institute, Max Planck Society;
Nano Life Science Institute (WPI-NanoLSI), Kanazawa University;

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2003.02574.pdf
(Preprint), 579KB

d0sm01138j.pdf
(Publisher version), 3MB

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Citation

Hosaka, Y., Komura, S., & Mikhailov, A. S. (2020). Mechanochemical enzymes and protein machines as hydrodynamic force dipoles: The active dimer model. Soft Matter, 16(47), 10734-10749. doi:10.1039/D0SM01138J.


Cite as: http://hdl.handle.net/21.11116/0000-0005-DC62-5
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.