Electrostatic model for protein/reverse micelle complexation
Bratko, D. ; Luzar, A. ; Chen, S. H.
College Park, Md. : American Institute of Physics (AIP)
Published 1988
College Park, Md. : American Institute of Physics (AIP)
Published 1988
| ISSN: |
1089-7690
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|---|---|
| Source: |
AIP Digital Archive
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| Topics: |
Physics
Chemistry and Pharmacology
|
| Notes: |
Thermodynamics of protein solubilization in water-in-oil microemulsions is analyzed in terms of the shell-and-core model for reverse micelles. The electrostatic contribution to the free energy of transfer of the protein from the aqueous solution to the microemulsion is determined via the solution of the nonlinear Poisson–Boltzmann equation for the protein/reverse micelle complex, for the protein-free micelle, and for the cell model of aqueous protein solution in equilibrium with the microemulsion. The electrolyte effect on the protein solubility in the microemulsion is studied. A good agreement between the predictions of the model and the known salting out effect of cytochrome-c in sodium di-2-ethylhexylsulfosuccinate AOT-water-in-isooctane microemulsion is observed.
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| Type of Medium: |
Electronic Resource
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| URL: |
| _version_ | 1798289751052124162 |
|---|---|
| autor | Bratko, D. Luzar, A. Chen, S. H. |
| autorsonst | Bratko, D. Luzar, A. Chen, S. H. |
| book_url | http://dx.doi.org/10.1063/1.455443 |
| datenlieferant | nat_lic_papers |
| hauptsatz | hsatz_simple |
| identnr | NLZ21890231X |
| issn | 1089-7690 |
| journal_name | The Journal of Chemical Physics |
| materialart | 1 |
| notes | Thermodynamics of protein solubilization in water-in-oil microemulsions is analyzed in terms of the shell-and-core model for reverse micelles. The electrostatic contribution to the free energy of transfer of the protein from the aqueous solution to the microemulsion is determined via the solution of the nonlinear Poisson–Boltzmann equation for the protein/reverse micelle complex, for the protein-free micelle, and for the cell model of aqueous protein solution in equilibrium with the microemulsion. The electrolyte effect on the protein solubility in the microemulsion is studied. A good agreement between the predictions of the model and the known salting out effect of cytochrome-c in sodium di-2-ethylhexylsulfosuccinate AOT-water-in-isooctane microemulsion is observed. |
| package_name | American Institute of Physics (AIP) |
| publikationsjahr_anzeige | 1988 |
| publikationsjahr_facette | 1988 |
| publikationsjahr_intervall | 8014:1985-1989 |
| publikationsjahr_sort | 1988 |
| publikationsort | College Park, Md. |
| publisher | American Institute of Physics (AIP) |
| reference | 89 (1988), S. 545-550 |
| search_space | articles |
| shingle_author_1 | Bratko, D. Luzar, A. Chen, S. H. |
| shingle_author_2 | Bratko, D. Luzar, A. Chen, S. H. |
| shingle_author_3 | Bratko, D. Luzar, A. Chen, S. H. |
| shingle_author_4 | Bratko, D. Luzar, A. Chen, S. H. |
| shingle_catch_all_1 | Bratko, D. Luzar, A. Chen, S. H. Electrostatic model for protein/reverse micelle complexation Thermodynamics of protein solubilization in water-in-oil microemulsions is analyzed in terms of the shell-and-core model for reverse micelles. The electrostatic contribution to the free energy of transfer of the protein from the aqueous solution to the microemulsion is determined via the solution of the nonlinear Poisson–Boltzmann equation for the protein/reverse micelle complex, for the protein-free micelle, and for the cell model of aqueous protein solution in equilibrium with the microemulsion. The electrolyte effect on the protein solubility in the microemulsion is studied. A good agreement between the predictions of the model and the known salting out effect of cytochrome-c in sodium di-2-ethylhexylsulfosuccinate AOT-water-in-isooctane microemulsion is observed. 1089-7690 10897690 American Institute of Physics (AIP) |
| shingle_catch_all_2 | Bratko, D. Luzar, A. Chen, S. H. Electrostatic model for protein/reverse micelle complexation Thermodynamics of protein solubilization in water-in-oil microemulsions is analyzed in terms of the shell-and-core model for reverse micelles. The electrostatic contribution to the free energy of transfer of the protein from the aqueous solution to the microemulsion is determined via the solution of the nonlinear Poisson–Boltzmann equation for the protein/reverse micelle complex, for the protein-free micelle, and for the cell model of aqueous protein solution in equilibrium with the microemulsion. The electrolyte effect on the protein solubility in the microemulsion is studied. A good agreement between the predictions of the model and the known salting out effect of cytochrome-c in sodium di-2-ethylhexylsulfosuccinate AOT-water-in-isooctane microemulsion is observed. 1089-7690 10897690 American Institute of Physics (AIP) |
| shingle_catch_all_3 | Bratko, D. Luzar, A. Chen, S. H. Electrostatic model for protein/reverse micelle complexation Thermodynamics of protein solubilization in water-in-oil microemulsions is analyzed in terms of the shell-and-core model for reverse micelles. The electrostatic contribution to the free energy of transfer of the protein from the aqueous solution to the microemulsion is determined via the solution of the nonlinear Poisson–Boltzmann equation for the protein/reverse micelle complex, for the protein-free micelle, and for the cell model of aqueous protein solution in equilibrium with the microemulsion. The electrolyte effect on the protein solubility in the microemulsion is studied. A good agreement between the predictions of the model and the known salting out effect of cytochrome-c in sodium di-2-ethylhexylsulfosuccinate AOT-water-in-isooctane microemulsion is observed. 1089-7690 10897690 American Institute of Physics (AIP) |
| shingle_catch_all_4 | Bratko, D. Luzar, A. Chen, S. H. Electrostatic model for protein/reverse micelle complexation Thermodynamics of protein solubilization in water-in-oil microemulsions is analyzed in terms of the shell-and-core model for reverse micelles. The electrostatic contribution to the free energy of transfer of the protein from the aqueous solution to the microemulsion is determined via the solution of the nonlinear Poisson–Boltzmann equation for the protein/reverse micelle complex, for the protein-free micelle, and for the cell model of aqueous protein solution in equilibrium with the microemulsion. The electrolyte effect on the protein solubility in the microemulsion is studied. A good agreement between the predictions of the model and the known salting out effect of cytochrome-c in sodium di-2-ethylhexylsulfosuccinate AOT-water-in-isooctane microemulsion is observed. 1089-7690 10897690 American Institute of Physics (AIP) |
| shingle_title_1 | Electrostatic model for protein/reverse micelle complexation |
| shingle_title_2 | Electrostatic model for protein/reverse micelle complexation |
| shingle_title_3 | Electrostatic model for protein/reverse micelle complexation |
| shingle_title_4 | Electrostatic model for protein/reverse micelle complexation |
| sigel_instance_filter | dkfz geomar wilbert ipn albert |
| source_archive | AIP Digital Archive |
| timestamp | 2024-05-06T08:05:48.576Z |
| titel | Electrostatic model for protein/reverse micelle complexation |
| titel_suche | Electrostatic model for protein/reverse micelle complexation |
| topic | U V |
| uid | nat_lic_papers_NLZ21890231X |