Modelling carbon dioxide molecule interacting with aquaglyceroporin and aquaporin-1 channels
Abstract Aquaporin (AQP) is a family of membrane proteins that enable water and small individual molecules to permeate cell membranes. Examples of these protein channels are aquaglyceroporin and aquaporin-1 (AQP1). Here, we investigate the permeability of carbon dioxide $$(\hbox {CO}_2)$$ through bo...
Ausführliche Beschreibung
Autor*in: |
Al Garalleh, Hakim [verfasserIn] |
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Format: |
Artikel |
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Sprache: |
Englisch |
Erschienen: |
2013 |
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Schlagwörter: |
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Anmerkung: |
© Springer Science+Business Media New York 2013 |
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Übergeordnetes Werk: |
Enthalten in: Journal of mathematical chemistry - Springer Netherlands, 1987, 51(2013), 9 vom: 27. Juli, Seite 2317-2327 |
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Übergeordnetes Werk: |
volume:51 ; year:2013 ; number:9 ; day:27 ; month:07 ; pages:2317-2327 |
Links: |
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DOI / URN: |
10.1007/s10910-013-0240-x |
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OLC206041850X |
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520 | |a Abstract Aquaporin (AQP) is a family of membrane proteins that enable water and small individual molecules to permeate cell membranes. Examples of these protein channels are aquaglyceroporin and aquaporin-1 (AQP1). Here, we investigate the permeability of carbon dioxide $$(\hbox {CO}_2)$$ through both aquglyceroporin and AQP1 channels and explain their selectivity mechanisms. We provide a mathematical model which determines the molecular interaction potential between carbon dioxide molecule and an AQP channel. We evaluate this interaction using two approaches, namely discrete-continuum and completed discrete approaches. Both calculations agree well and our results indicate the acceptance of $$(\hbox {CO}_2)$$ molecule into these channels which is in good agreement with other recent studies. | ||
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10.1007/s10910-013-0240-x doi (DE-627)OLC206041850X (DE-He213)s10910-013-0240-x-p DE-627 ger DE-627 rakwb eng 510 540 VZ Al Garalleh, Hakim verfasserin aut Modelling carbon dioxide molecule interacting with aquaglyceroporin and aquaporin-1 channels 2013 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer Science+Business Media New York 2013 Abstract Aquaporin (AQP) is a family of membrane proteins that enable water and small individual molecules to permeate cell membranes. Examples of these protein channels are aquaglyceroporin and aquaporin-1 (AQP1). Here, we investigate the permeability of carbon dioxide $$(\hbox {CO}_2)$$ through both aquglyceroporin and AQP1 channels and explain their selectivity mechanisms. We provide a mathematical model which determines the molecular interaction potential between carbon dioxide molecule and an AQP channel. We evaluate this interaction using two approaches, namely discrete-continuum and completed discrete approaches. Both calculations agree well and our results indicate the acceptance of $$(\hbox {CO}_2)$$ molecule into these channels which is in good agreement with other recent studies. Aquaporins (AQPs) Aquaporin-1 (AQP1) Aquaglyceroporin (GlpF) Lennard–Jones potential Van der Waals interaction Carbon dioxide Thamwattana, Ngamta aut Cox, Barry J. aut Hill, James M. aut Enthalten in Journal of mathematical chemistry Springer Netherlands, 1987 51(2013), 9 vom: 27. Juli, Seite 2317-2327 (DE-627)129246441 (DE-600)59132-4 (DE-576)27906036X 0259-9791 nnns volume:51 year:2013 number:9 day:27 month:07 pages:2317-2327 https://doi.org/10.1007/s10910-013-0240-x lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-CHE SSG-OLC-MAT SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-MAT GBV_ILN_70 GBV_ILN_4012 AR 51 2013 9 27 07 2317-2327 |
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10.1007/s10910-013-0240-x doi (DE-627)OLC206041850X (DE-He213)s10910-013-0240-x-p DE-627 ger DE-627 rakwb eng 510 540 VZ Al Garalleh, Hakim verfasserin aut Modelling carbon dioxide molecule interacting with aquaglyceroporin and aquaporin-1 channels 2013 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer Science+Business Media New York 2013 Abstract Aquaporin (AQP) is a family of membrane proteins that enable water and small individual molecules to permeate cell membranes. Examples of these protein channels are aquaglyceroporin and aquaporin-1 (AQP1). Here, we investigate the permeability of carbon dioxide $$(\hbox {CO}_2)$$ through both aquglyceroporin and AQP1 channels and explain their selectivity mechanisms. We provide a mathematical model which determines the molecular interaction potential between carbon dioxide molecule and an AQP channel. We evaluate this interaction using two approaches, namely discrete-continuum and completed discrete approaches. Both calculations agree well and our results indicate the acceptance of $$(\hbox {CO}_2)$$ molecule into these channels which is in good agreement with other recent studies. Aquaporins (AQPs) Aquaporin-1 (AQP1) Aquaglyceroporin (GlpF) Lennard–Jones potential Van der Waals interaction Carbon dioxide Thamwattana, Ngamta aut Cox, Barry J. aut Hill, James M. aut Enthalten in Journal of mathematical chemistry Springer Netherlands, 1987 51(2013), 9 vom: 27. Juli, Seite 2317-2327 (DE-627)129246441 (DE-600)59132-4 (DE-576)27906036X 0259-9791 nnns volume:51 year:2013 number:9 day:27 month:07 pages:2317-2327 https://doi.org/10.1007/s10910-013-0240-x lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-CHE SSG-OLC-MAT SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-MAT GBV_ILN_70 GBV_ILN_4012 AR 51 2013 9 27 07 2317-2327 |
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10.1007/s10910-013-0240-x doi (DE-627)OLC206041850X (DE-He213)s10910-013-0240-x-p DE-627 ger DE-627 rakwb eng 510 540 VZ Al Garalleh, Hakim verfasserin aut Modelling carbon dioxide molecule interacting with aquaglyceroporin and aquaporin-1 channels 2013 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer Science+Business Media New York 2013 Abstract Aquaporin (AQP) is a family of membrane proteins that enable water and small individual molecules to permeate cell membranes. Examples of these protein channels are aquaglyceroporin and aquaporin-1 (AQP1). Here, we investigate the permeability of carbon dioxide $$(\hbox {CO}_2)$$ through both aquglyceroporin and AQP1 channels and explain their selectivity mechanisms. We provide a mathematical model which determines the molecular interaction potential between carbon dioxide molecule and an AQP channel. We evaluate this interaction using two approaches, namely discrete-continuum and completed discrete approaches. Both calculations agree well and our results indicate the acceptance of $$(\hbox {CO}_2)$$ molecule into these channels which is in good agreement with other recent studies. Aquaporins (AQPs) Aquaporin-1 (AQP1) Aquaglyceroporin (GlpF) Lennard–Jones potential Van der Waals interaction Carbon dioxide Thamwattana, Ngamta aut Cox, Barry J. aut Hill, James M. aut Enthalten in Journal of mathematical chemistry Springer Netherlands, 1987 51(2013), 9 vom: 27. Juli, Seite 2317-2327 (DE-627)129246441 (DE-600)59132-4 (DE-576)27906036X 0259-9791 nnns volume:51 year:2013 number:9 day:27 month:07 pages:2317-2327 https://doi.org/10.1007/s10910-013-0240-x lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-CHE SSG-OLC-MAT SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-MAT GBV_ILN_70 GBV_ILN_4012 AR 51 2013 9 27 07 2317-2327 |
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10.1007/s10910-013-0240-x doi (DE-627)OLC206041850X (DE-He213)s10910-013-0240-x-p DE-627 ger DE-627 rakwb eng 510 540 VZ Al Garalleh, Hakim verfasserin aut Modelling carbon dioxide molecule interacting with aquaglyceroporin and aquaporin-1 channels 2013 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer Science+Business Media New York 2013 Abstract Aquaporin (AQP) is a family of membrane proteins that enable water and small individual molecules to permeate cell membranes. Examples of these protein channels are aquaglyceroporin and aquaporin-1 (AQP1). Here, we investigate the permeability of carbon dioxide $$(\hbox {CO}_2)$$ through both aquglyceroporin and AQP1 channels and explain their selectivity mechanisms. We provide a mathematical model which determines the molecular interaction potential between carbon dioxide molecule and an AQP channel. We evaluate this interaction using two approaches, namely discrete-continuum and completed discrete approaches. Both calculations agree well and our results indicate the acceptance of $$(\hbox {CO}_2)$$ molecule into these channels which is in good agreement with other recent studies. Aquaporins (AQPs) Aquaporin-1 (AQP1) Aquaglyceroporin (GlpF) Lennard–Jones potential Van der Waals interaction Carbon dioxide Thamwattana, Ngamta aut Cox, Barry J. aut Hill, James M. aut Enthalten in Journal of mathematical chemistry Springer Netherlands, 1987 51(2013), 9 vom: 27. Juli, Seite 2317-2327 (DE-627)129246441 (DE-600)59132-4 (DE-576)27906036X 0259-9791 nnns volume:51 year:2013 number:9 day:27 month:07 pages:2317-2327 https://doi.org/10.1007/s10910-013-0240-x lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-CHE SSG-OLC-MAT SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-MAT GBV_ILN_70 GBV_ILN_4012 AR 51 2013 9 27 07 2317-2327 |
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10.1007/s10910-013-0240-x doi (DE-627)OLC206041850X (DE-He213)s10910-013-0240-x-p DE-627 ger DE-627 rakwb eng 510 540 VZ Al Garalleh, Hakim verfasserin aut Modelling carbon dioxide molecule interacting with aquaglyceroporin and aquaporin-1 channels 2013 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer Science+Business Media New York 2013 Abstract Aquaporin (AQP) is a family of membrane proteins that enable water and small individual molecules to permeate cell membranes. Examples of these protein channels are aquaglyceroporin and aquaporin-1 (AQP1). Here, we investigate the permeability of carbon dioxide $$(\hbox {CO}_2)$$ through both aquglyceroporin and AQP1 channels and explain their selectivity mechanisms. We provide a mathematical model which determines the molecular interaction potential between carbon dioxide molecule and an AQP channel. We evaluate this interaction using two approaches, namely discrete-continuum and completed discrete approaches. Both calculations agree well and our results indicate the acceptance of $$(\hbox {CO}_2)$$ molecule into these channels which is in good agreement with other recent studies. Aquaporins (AQPs) Aquaporin-1 (AQP1) Aquaglyceroporin (GlpF) Lennard–Jones potential Van der Waals interaction Carbon dioxide Thamwattana, Ngamta aut Cox, Barry J. aut Hill, James M. aut Enthalten in Journal of mathematical chemistry Springer Netherlands, 1987 51(2013), 9 vom: 27. Juli, Seite 2317-2327 (DE-627)129246441 (DE-600)59132-4 (DE-576)27906036X 0259-9791 nnns volume:51 year:2013 number:9 day:27 month:07 pages:2317-2327 https://doi.org/10.1007/s10910-013-0240-x lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-CHE SSG-OLC-MAT SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-MAT GBV_ILN_70 GBV_ILN_4012 AR 51 2013 9 27 07 2317-2327 |
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Modelling carbon dioxide molecule interacting with aquaglyceroporin and aquaporin-1 channels |
abstract |
Abstract Aquaporin (AQP) is a family of membrane proteins that enable water and small individual molecules to permeate cell membranes. Examples of these protein channels are aquaglyceroporin and aquaporin-1 (AQP1). Here, we investigate the permeability of carbon dioxide $$(\hbox {CO}_2)$$ through both aquglyceroporin and AQP1 channels and explain their selectivity mechanisms. We provide a mathematical model which determines the molecular interaction potential between carbon dioxide molecule and an AQP channel. We evaluate this interaction using two approaches, namely discrete-continuum and completed discrete approaches. Both calculations agree well and our results indicate the acceptance of $$(\hbox {CO}_2)$$ molecule into these channels which is in good agreement with other recent studies. © Springer Science+Business Media New York 2013 |
abstractGer |
Abstract Aquaporin (AQP) is a family of membrane proteins that enable water and small individual molecules to permeate cell membranes. Examples of these protein channels are aquaglyceroporin and aquaporin-1 (AQP1). Here, we investigate the permeability of carbon dioxide $$(\hbox {CO}_2)$$ through both aquglyceroporin and AQP1 channels and explain their selectivity mechanisms. We provide a mathematical model which determines the molecular interaction potential between carbon dioxide molecule and an AQP channel. We evaluate this interaction using two approaches, namely discrete-continuum and completed discrete approaches. Both calculations agree well and our results indicate the acceptance of $$(\hbox {CO}_2)$$ molecule into these channels which is in good agreement with other recent studies. © Springer Science+Business Media New York 2013 |
abstract_unstemmed |
Abstract Aquaporin (AQP) is a family of membrane proteins that enable water and small individual molecules to permeate cell membranes. Examples of these protein channels are aquaglyceroporin and aquaporin-1 (AQP1). Here, we investigate the permeability of carbon dioxide $$(\hbox {CO}_2)$$ through both aquglyceroporin and AQP1 channels and explain their selectivity mechanisms. We provide a mathematical model which determines the molecular interaction potential between carbon dioxide molecule and an AQP channel. We evaluate this interaction using two approaches, namely discrete-continuum and completed discrete approaches. Both calculations agree well and our results indicate the acceptance of $$(\hbox {CO}_2)$$ molecule into these channels which is in good agreement with other recent studies. © Springer Science+Business Media New York 2013 |
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container_issue |
9 |
title_short |
Modelling carbon dioxide molecule interacting with aquaglyceroporin and aquaporin-1 channels |
url |
https://doi.org/10.1007/s10910-013-0240-x |
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author2 |
Thamwattana, Ngamta Cox, Barry J. Hill, James M. |
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Thamwattana, Ngamta Cox, Barry J. Hill, James M. |
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doi_str |
10.1007/s10910-013-0240-x |
up_date |
2024-07-04T01:17:44.436Z |
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