The effect of boundary conditions on the mesoscopic lattice Boltzmann method: Case study of a reaction-diffusion based model for Min-protein oscillation
Min-protein oscillation in Escherichia coli has an essential role in controlling the accurate placement of the cell division septum at the middle-cell zone of the bacteria. This biochemical process has been successfully described by a set of reaction-diffusion equations at the macroscopic level. The...
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th-cmuir.6653943832-385852015-06-16T07:53:26Z The effect of boundary conditions on the mesoscopic lattice Boltzmann method: Case study of a reaction-diffusion based model for Min-protein oscillation Ngamsaad,W. Kanthang,P. Modchang,C. Sriyab,S. Triampo,W. Applied Mathematics Computational Mathematics Min-protein oscillation in Escherichia coli has an essential role in controlling the accurate placement of the cell division septum at the middle-cell zone of the bacteria. This biochemical process has been successfully described by a set of reaction-diffusion equations at the macroscopic level. The lattice Boltzmann method (LBM) has been used to simulate Min-protein oscillation and proved to recover the correct macroscopic equations. In this present work, we studied the effects of LBM boundary conditions (BC) on Min-protein oscillation. The impact of diffusion and reaction dynamics on BCs was also investigated. It was found that the mirror-image BC is a suitable boundary treatment for this Min-protein model. The physical significance of the results is extensively discussed. © 2010 Elsevier Inc. All rights reserved. 2015-06-16T07:53:26Z 2015-06-16T07:53:26Z 2010-11-15 Article 00963003 2-s2.0-77957978078 10.1016/j.amc.2010.07.033 http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=77957978078&origin=inward http://cmuir.cmu.ac.th/handle/6653943832/38585 Elsevier Inc. |
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Applied Mathematics Computational Mathematics Ngamsaad,W. Kanthang,P. Modchang,C. Sriyab,S. Triampo,W. The effect of boundary conditions on the mesoscopic lattice Boltzmann method: Case study of a reaction-diffusion based model for Min-protein oscillation |
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Min-protein oscillation in Escherichia coli has an essential role in controlling the accurate placement of the cell division septum at the middle-cell zone of the bacteria. This biochemical process has been successfully described by a set of reaction-diffusion equations at the macroscopic level. The lattice Boltzmann method (LBM) has been used to simulate Min-protein oscillation and proved to recover the correct macroscopic equations. In this present work, we studied the effects of LBM boundary conditions (BC) on Min-protein oscillation. The impact of diffusion and reaction dynamics on BCs was also investigated. It was found that the mirror-image BC is a suitable boundary treatment for this Min-protein model. The physical significance of the results is extensively discussed. © 2010 Elsevier Inc. All rights reserved. |
format |
Article |
author |
Ngamsaad,W. Kanthang,P. Modchang,C. Sriyab,S. Triampo,W. |
author_facet |
Ngamsaad,W. Kanthang,P. Modchang,C. Sriyab,S. Triampo,W. |
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Ngamsaad,W. |
title |
The effect of boundary conditions on the mesoscopic lattice Boltzmann method: Case study of a reaction-diffusion based model for Min-protein oscillation |
title_short |
The effect of boundary conditions on the mesoscopic lattice Boltzmann method: Case study of a reaction-diffusion based model for Min-protein oscillation |
title_full |
The effect of boundary conditions on the mesoscopic lattice Boltzmann method: Case study of a reaction-diffusion based model for Min-protein oscillation |
title_fullStr |
The effect of boundary conditions on the mesoscopic lattice Boltzmann method: Case study of a reaction-diffusion based model for Min-protein oscillation |
title_full_unstemmed |
The effect of boundary conditions on the mesoscopic lattice Boltzmann method: Case study of a reaction-diffusion based model for Min-protein oscillation |
title_sort |
effect of boundary conditions on the mesoscopic lattice boltzmann method: case study of a reaction-diffusion based model for min-protein oscillation |
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Elsevier Inc. |
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2015 |
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http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=77957978078&origin=inward http://cmuir.cmu.ac.th/handle/6653943832/38585 |
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