Temperature-mediated switching of protectant-denaturant behavior of trimethylamine-N-oxide and consequences on protein stability from a replica exchange molecular dynamics simulation study
The detailed mechanism of protein folding-unfolding processes with the aid of osmolytes has been a leading topic of discussion over many decades. We have used replica-exchange molecular dynamics simulation to propose the molecular mechanism of interaction of a 20-residue mini-protein with urea and t...
Ausführliche Beschreibung
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| Autor*in: |
Borgohain, Gargi [verfasserIn] |
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| Format: |
Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2017 |
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| Rechteinformationen: |
Nutzungsrecht: © 2016 Informa UK Limited, trading as Taylor & Francis Group 2016 |
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| Schlagwörter: |
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| Übergeordnetes Werk: |
Enthalten in: Molecular simulation - New York, NY [u.a.] : Gordon and Breach, 1987, 43(2017), 1, Seite 52-13 |
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| Übergeordnetes Werk: |
volume:43 ; year:2017 ; number:1 ; pages:52-13 |
| Links: |
|---|
| DOI / URN: |
10.1080/08927022.2016.1233546 |
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| 520 | |a The detailed mechanism of protein folding-unfolding processes with the aid of osmolytes has been a leading topic of discussion over many decades. We have used replica-exchange molecular dynamics simulation to propose the molecular mechanism of interaction of a 20-residue mini-protein with urea and trimethylamine N-oxide (TMAO) that act as denaturing and protecting osmolyte, respectively, in binary osmolyte solutions. Urea is found to exert its action by interacting directly with the protein residues. Temperature tolerance of TMAO's action is particularly emphasised in this study. At lower range of temperature, TMAO acts as a successful protein protectant. Interestingly, the study discloses the tendency of TMAO molecules to prefer self-association at the protein surface at elevated temperature. A greater number of TMAO molecules in the protein hydration shell at higher temperature is also observed. Dihedral angle principal component analysis and free energy landscape plots sampled all possible conformations adopted by the protein that reveal highly folded behaviour of the protein in pure water and binary TMAO solutions and highly unfolded behaviour in presence of urea. | ||
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10.1080/08927022.2016.1233546 doi PQ20161201 (DE-627)OLC1985627566 (DE-599)GBVOLC1985627566 (PRQ)c1267-ed888566678c7584b13edf22b9a136a3248cc861f7aa2ab87f6ffecbaf59921d0 (KEY)0163460720170000043000100052temperaturemediatedswitchingofprotectantdenaturant DE-627 ger DE-627 rakwb eng 530 600 DNB Borgohain, Gargi verfasserin aut Temperature-mediated switching of protectant-denaturant behavior of trimethylamine-N-oxide and consequences on protein stability from a replica exchange molecular dynamics simulation study 2017 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier The detailed mechanism of protein folding-unfolding processes with the aid of osmolytes has been a leading topic of discussion over many decades. We have used replica-exchange molecular dynamics simulation to propose the molecular mechanism of interaction of a 20-residue mini-protein with urea and trimethylamine N-oxide (TMAO) that act as denaturing and protecting osmolyte, respectively, in binary osmolyte solutions. Urea is found to exert its action by interacting directly with the protein residues. Temperature tolerance of TMAO's action is particularly emphasised in this study. At lower range of temperature, TMAO acts as a successful protein protectant. Interestingly, the study discloses the tendency of TMAO molecules to prefer self-association at the protein surface at elevated temperature. A greater number of TMAO molecules in the protein hydration shell at higher temperature is also observed. Dihedral angle principal component analysis and free energy landscape plots sampled all possible conformations adopted by the protein that reveal highly folded behaviour of the protein in pure water and binary TMAO solutions and highly unfolded behaviour in presence of urea. Nutzungsrecht: © 2016 Informa UK Limited, trading as Taylor & Francis Group 2016 osmolyte REMD urea TMAO (trimethylamine protein Paul, Sandip oth Enthalten in Molecular simulation New York, NY [u.a.] : Gordon and Breach, 1987 43(2017), 1, Seite 52-13 (DE-627)165660120 (DE-600)636828-1 (DE-576)02291384X 0892-7022 nnns volume:43 year:2017 number:1 pages:52-13 http://dx.doi.org/10.1080/08927022.2016.1233546 Volltext http://www.tandfonline.com/doi/abs/10.1080/08927022.2016.1233546 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-PHY GBV_ILN_70 AR 43 2017 1 52-13 |
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10.1080/08927022.2016.1233546 doi PQ20161201 (DE-627)OLC1985627566 (DE-599)GBVOLC1985627566 (PRQ)c1267-ed888566678c7584b13edf22b9a136a3248cc861f7aa2ab87f6ffecbaf59921d0 (KEY)0163460720170000043000100052temperaturemediatedswitchingofprotectantdenaturant DE-627 ger DE-627 rakwb eng 530 600 DNB Borgohain, Gargi verfasserin aut Temperature-mediated switching of protectant-denaturant behavior of trimethylamine-N-oxide and consequences on protein stability from a replica exchange molecular dynamics simulation study 2017 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier The detailed mechanism of protein folding-unfolding processes with the aid of osmolytes has been a leading topic of discussion over many decades. We have used replica-exchange molecular dynamics simulation to propose the molecular mechanism of interaction of a 20-residue mini-protein with urea and trimethylamine N-oxide (TMAO) that act as denaturing and protecting osmolyte, respectively, in binary osmolyte solutions. Urea is found to exert its action by interacting directly with the protein residues. Temperature tolerance of TMAO's action is particularly emphasised in this study. At lower range of temperature, TMAO acts as a successful protein protectant. Interestingly, the study discloses the tendency of TMAO molecules to prefer self-association at the protein surface at elevated temperature. A greater number of TMAO molecules in the protein hydration shell at higher temperature is also observed. Dihedral angle principal component analysis and free energy landscape plots sampled all possible conformations adopted by the protein that reveal highly folded behaviour of the protein in pure water and binary TMAO solutions and highly unfolded behaviour in presence of urea. Nutzungsrecht: © 2016 Informa UK Limited, trading as Taylor & Francis Group 2016 osmolyte REMD urea TMAO (trimethylamine protein Paul, Sandip oth Enthalten in Molecular simulation New York, NY [u.a.] : Gordon and Breach, 1987 43(2017), 1, Seite 52-13 (DE-627)165660120 (DE-600)636828-1 (DE-576)02291384X 0892-7022 nnns volume:43 year:2017 number:1 pages:52-13 http://dx.doi.org/10.1080/08927022.2016.1233546 Volltext http://www.tandfonline.com/doi/abs/10.1080/08927022.2016.1233546 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-PHY GBV_ILN_70 AR 43 2017 1 52-13 |
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10.1080/08927022.2016.1233546 doi PQ20161201 (DE-627)OLC1985627566 (DE-599)GBVOLC1985627566 (PRQ)c1267-ed888566678c7584b13edf22b9a136a3248cc861f7aa2ab87f6ffecbaf59921d0 (KEY)0163460720170000043000100052temperaturemediatedswitchingofprotectantdenaturant DE-627 ger DE-627 rakwb eng 530 600 DNB Borgohain, Gargi verfasserin aut Temperature-mediated switching of protectant-denaturant behavior of trimethylamine-N-oxide and consequences on protein stability from a replica exchange molecular dynamics simulation study 2017 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier The detailed mechanism of protein folding-unfolding processes with the aid of osmolytes has been a leading topic of discussion over many decades. We have used replica-exchange molecular dynamics simulation to propose the molecular mechanism of interaction of a 20-residue mini-protein with urea and trimethylamine N-oxide (TMAO) that act as denaturing and protecting osmolyte, respectively, in binary osmolyte solutions. Urea is found to exert its action by interacting directly with the protein residues. Temperature tolerance of TMAO's action is particularly emphasised in this study. At lower range of temperature, TMAO acts as a successful protein protectant. Interestingly, the study discloses the tendency of TMAO molecules to prefer self-association at the protein surface at elevated temperature. A greater number of TMAO molecules in the protein hydration shell at higher temperature is also observed. Dihedral angle principal component analysis and free energy landscape plots sampled all possible conformations adopted by the protein that reveal highly folded behaviour of the protein in pure water and binary TMAO solutions and highly unfolded behaviour in presence of urea. Nutzungsrecht: © 2016 Informa UK Limited, trading as Taylor & Francis Group 2016 osmolyte REMD urea TMAO (trimethylamine protein Paul, Sandip oth Enthalten in Molecular simulation New York, NY [u.a.] : Gordon and Breach, 1987 43(2017), 1, Seite 52-13 (DE-627)165660120 (DE-600)636828-1 (DE-576)02291384X 0892-7022 nnns volume:43 year:2017 number:1 pages:52-13 http://dx.doi.org/10.1080/08927022.2016.1233546 Volltext http://www.tandfonline.com/doi/abs/10.1080/08927022.2016.1233546 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-PHY GBV_ILN_70 AR 43 2017 1 52-13 |
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10.1080/08927022.2016.1233546 doi PQ20161201 (DE-627)OLC1985627566 (DE-599)GBVOLC1985627566 (PRQ)c1267-ed888566678c7584b13edf22b9a136a3248cc861f7aa2ab87f6ffecbaf59921d0 (KEY)0163460720170000043000100052temperaturemediatedswitchingofprotectantdenaturant DE-627 ger DE-627 rakwb eng 530 600 DNB Borgohain, Gargi verfasserin aut Temperature-mediated switching of protectant-denaturant behavior of trimethylamine-N-oxide and consequences on protein stability from a replica exchange molecular dynamics simulation study 2017 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier The detailed mechanism of protein folding-unfolding processes with the aid of osmolytes has been a leading topic of discussion over many decades. We have used replica-exchange molecular dynamics simulation to propose the molecular mechanism of interaction of a 20-residue mini-protein with urea and trimethylamine N-oxide (TMAO) that act as denaturing and protecting osmolyte, respectively, in binary osmolyte solutions. Urea is found to exert its action by interacting directly with the protein residues. Temperature tolerance of TMAO's action is particularly emphasised in this study. At lower range of temperature, TMAO acts as a successful protein protectant. Interestingly, the study discloses the tendency of TMAO molecules to prefer self-association at the protein surface at elevated temperature. A greater number of TMAO molecules in the protein hydration shell at higher temperature is also observed. Dihedral angle principal component analysis and free energy landscape plots sampled all possible conformations adopted by the protein that reveal highly folded behaviour of the protein in pure water and binary TMAO solutions and highly unfolded behaviour in presence of urea. Nutzungsrecht: © 2016 Informa UK Limited, trading as Taylor & Francis Group 2016 osmolyte REMD urea TMAO (trimethylamine protein Paul, Sandip oth Enthalten in Molecular simulation New York, NY [u.a.] : Gordon and Breach, 1987 43(2017), 1, Seite 52-13 (DE-627)165660120 (DE-600)636828-1 (DE-576)02291384X 0892-7022 nnns volume:43 year:2017 number:1 pages:52-13 http://dx.doi.org/10.1080/08927022.2016.1233546 Volltext http://www.tandfonline.com/doi/abs/10.1080/08927022.2016.1233546 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-PHY GBV_ILN_70 AR 43 2017 1 52-13 |
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Borgohain, Gargi |
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| author-letter |
Borgohain, Gargi |
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10.1080/08927022.2016.1233546 |
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530 600 |
| title_sort |
temperature-mediated switching of protectant-denaturant behavior of trimethylamine-n-oxide and consequences on protein stability from a replica exchange molecular dynamics simulation study |
| title_auth |
Temperature-mediated switching of protectant-denaturant behavior of trimethylamine-N-oxide and consequences on protein stability from a replica exchange molecular dynamics simulation study |
| abstract |
The detailed mechanism of protein folding-unfolding processes with the aid of osmolytes has been a leading topic of discussion over many decades. We have used replica-exchange molecular dynamics simulation to propose the molecular mechanism of interaction of a 20-residue mini-protein with urea and trimethylamine N-oxide (TMAO) that act as denaturing and protecting osmolyte, respectively, in binary osmolyte solutions. Urea is found to exert its action by interacting directly with the protein residues. Temperature tolerance of TMAO's action is particularly emphasised in this study. At lower range of temperature, TMAO acts as a successful protein protectant. Interestingly, the study discloses the tendency of TMAO molecules to prefer self-association at the protein surface at elevated temperature. A greater number of TMAO molecules in the protein hydration shell at higher temperature is also observed. Dihedral angle principal component analysis and free energy landscape plots sampled all possible conformations adopted by the protein that reveal highly folded behaviour of the protein in pure water and binary TMAO solutions and highly unfolded behaviour in presence of urea. |
| abstractGer |
The detailed mechanism of protein folding-unfolding processes with the aid of osmolytes has been a leading topic of discussion over many decades. We have used replica-exchange molecular dynamics simulation to propose the molecular mechanism of interaction of a 20-residue mini-protein with urea and trimethylamine N-oxide (TMAO) that act as denaturing and protecting osmolyte, respectively, in binary osmolyte solutions. Urea is found to exert its action by interacting directly with the protein residues. Temperature tolerance of TMAO's action is particularly emphasised in this study. At lower range of temperature, TMAO acts as a successful protein protectant. Interestingly, the study discloses the tendency of TMAO molecules to prefer self-association at the protein surface at elevated temperature. A greater number of TMAO molecules in the protein hydration shell at higher temperature is also observed. Dihedral angle principal component analysis and free energy landscape plots sampled all possible conformations adopted by the protein that reveal highly folded behaviour of the protein in pure water and binary TMAO solutions and highly unfolded behaviour in presence of urea. |
| abstract_unstemmed |
The detailed mechanism of protein folding-unfolding processes with the aid of osmolytes has been a leading topic of discussion over many decades. We have used replica-exchange molecular dynamics simulation to propose the molecular mechanism of interaction of a 20-residue mini-protein with urea and trimethylamine N-oxide (TMAO) that act as denaturing and protecting osmolyte, respectively, in binary osmolyte solutions. Urea is found to exert its action by interacting directly with the protein residues. Temperature tolerance of TMAO's action is particularly emphasised in this study. At lower range of temperature, TMAO acts as a successful protein protectant. Interestingly, the study discloses the tendency of TMAO molecules to prefer self-association at the protein surface at elevated temperature. A greater number of TMAO molecules in the protein hydration shell at higher temperature is also observed. Dihedral angle principal component analysis and free energy landscape plots sampled all possible conformations adopted by the protein that reveal highly folded behaviour of the protein in pure water and binary TMAO solutions and highly unfolded behaviour in presence of urea. |
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| title_short |
Temperature-mediated switching of protectant-denaturant behavior of trimethylamine-N-oxide and consequences on protein stability from a replica exchange molecular dynamics simulation study |
| url |
http://dx.doi.org/10.1080/08927022.2016.1233546 http://www.tandfonline.com/doi/abs/10.1080/08927022.2016.1233546 |
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Paul, Sandip |
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10.1080/08927022.2016.1233546 |
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2024-07-04T03:15:54.374Z |
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7.400589 |