Journal article
Diffusion of an enzyme: the role of fluctuation-induced hydrodynamic coupling
- Abstract:
- The effect of conformational fluctuations of modular macromolecules, such as enzymes, on their diffusion properties is addressed using a simple generic model of an asymmetric dumbbell made of two hydrodynamically coupled subunits. It is shown that equilibrium fluctuations can lead to an interplay between the internal and the external degrees of freedom and give rise to negative contributions to the overall diffusion coefficient. Considering that this model enzyme explores a mechanochemical cycle, we show how substrate binding and unbinding affects its internal fluctuations, and how this can result in an enhancement of the overall diffusion coefficient of the molecule. These theoretical predictions are successfully confronted with recent measurements of enzyme diffusion in dilute conditions using fluorescence correlation spectroscopy.
- Publication status:
- Published
- Peer review status:
- Peer reviewed
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Access Document
- Files:
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(Preview, Accepted manuscript, pdf, 634.3KB, Terms of use)
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- Publisher copy:
- 10.1209/0295-5075/119/40002
Authors
- Publisher:
- EPL Association
- Journal:
- EPL More from this journal
- Volume:
- 119
- Issue:
- 4
- Article number:
- 40002
- Publication date:
- 2017-11-03
- Acceptance date:
- 2017-10-11
- DOI:
- EISSN:
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1286-4854
- ISSN:
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0295-5075
- Language:
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English
- Keywords:
- Pubs id:
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pubs:810046
- UUID:
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uuid:21c08ddf-f0c7-4df9-a789-88af4a04b7e9
- Local pid:
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pubs:810046
- Source identifiers:
-
810046
- Deposit date:
-
2019-05-22
Terms of use
- Copyright holder:
- EPL Association
- Copyright date:
- 2017
- Rights statement:
- © EPLA, 2017
- Notes:
- This is the accepted manuscript version of the article. The final version is available online from EPL Association at: 10.1209/0295-5075/119/40002
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