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

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.

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Item Permalink: https://hdl.handle.net/21.11116/0000-0005-DC62-5 Version Permalink: https://hdl.handle.net/21.11116/0000-0007-9C93-3
Genre: Journal Article

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 Creators:
Hosaka, Yuto1, Author
Komura, Shigeyuki1, Author
Mikhailov, Alexander S.2, 3, Author           
Affiliations:
1Department of Chemistry, Graduate School of Science, Tokyo Metropolitan University, Tokyo 192-0397, Japan, ou_persistent22              
2Physical Chemistry, Fritz Haber Institute, Max Planck Society, ou_634546              
3Nano Life Science Institute (WPI-NanoLSI), Kanazawa University, Kakuma-machi, Kanazawa, 920-1192, Japan, ou_persistent22              

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Free keywords: Condensed Matter, Soft Condensed Matter, cond-mat.soft
 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.

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Language(s): eng - English
 Dates: 2020-03-052020-06-222020-09-142020-12-21
 Publication Status: Published online
 Pages: 16
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: arXiv: 2003.02574
URI: http://arxiv.org/abs/2003.02574
DOI: 10.1039/D0SM01138J
 Degree: -

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Title: Soft Matter
  Abbreviation : Soft Matter
Source Genre: Journal
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Publ. Info: Cambridge, UK : Royal Society of Chemistry
Pages: 16 Volume / Issue: 16 (47) Sequence Number: - Start / End Page: 10734 - 10749 Identifier: ISSN: 1744-683X
CoNE: https://pure.mpg.de/cone/journals/resource/1744-683X