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

MPG-Autoren
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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
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d0sm01138j.pdf
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Zitation

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.


Zitierlink: https://hdl.handle.net/21.11116/0000-0005-DC62-5
Zusammenfassung
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.