Journal article
Chemical and hydrodynamic alignment of an enzyme
- 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.
- Publication status:
- Published
- Peer review status:
- Peer reviewed
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- Files:
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(Preview, Version of record, 1.3MB, Terms of use)
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(Preview, Accepted manuscript, pdf, 826.6KB, Terms of use)
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- Publisher copy:
- 10.1063/1.5081717
Authors
- Publisher:
- AIP Publishing
- Journal:
- Journal of Chemical Physics More from this journal
- Volume:
- 150
- Issue:
- 11
- Article number:
- 115102
- Publication date:
- 2019-03-18
- Acceptance date:
- 2019-02-26
- DOI:
- EISSN:
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1089-7690
- ISSN:
-
0021-9606
- Pmid:
-
30901991
- Language:
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English
- Keywords:
- Pubs id:
-
pubs:985311
- UUID:
-
uuid:bc8da60a-d7ed-4fc7-8bf6-9d3fe04a3cb3
- Local pid:
-
pubs:985311
- Source identifiers:
-
985311
- Deposit date:
-
2019-05-29
Terms of use
- Copyright holder:
- Adeleke-Larodo et al
- Copyright date:
- 2019
- Notes:
-
Copyright © 2019 Authors. Published under license by AIP Publishing.
Note: a correction exists for this article, originally published and available at: https://doi.org/10.1063/1.5097948
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