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  Chemical and hydrodynamic alignment of an enzyme

Adeleke-Larodo, T., Agudo-Canalejo, J., & Golestanian, R. (2019). Chemical and hydrodynamic alignment of an enzyme. The Journal of Chemical Physics, 150(11): 11502. doi:10.1063/1.5081717.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0003-4053-7 Version Permalink: http://hdl.handle.net/21.11116/0000-0003-4054-6
Genre: Journal Article

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Adeleke-Larodo, T., Author
Agudo-Canalejo, J., Author
Golestanian, Ramin1, Author              
Affiliations:
1Department of Living Matter Physics, Max Planck Institute for Dynamics and Self-Organization, Max Planck Society, ou_2570692              

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 Abstract: Motivated by the implications of the complex and dynamic modular geometry of an enzyme on its motion, we investigate the effect of combining long-range internal and external hydrodynamic interactions due to thermal fluctuations with short-range surface interactions. An asymmetric dumbbell consisting of two unequal subunits, in a nonuniform suspension of a solute with which it interacts via hydrodynamic interactions as well as non-contact surface interactions, is shown to have two alignment mechanisms due to the two types of interactions. In addition to alignment, the chemical gradient results in a drift velocity that is modified by hydrodynamic interactions between the constituents of the enzyme.

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Language(s): eng - English
 Dates: 2019-03-182019
 Publication Status: Published in print
 Pages: -
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 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1063/1.5081717
 Degree: -

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Title: The Journal of Chemical Physics
Source Genre: Journal
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Pages: 11 Volume / Issue: 150 (11) Sequence Number: 11502 Start / End Page: - Identifier: -