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Protein-Protein Interactions in Concentrated Electrolyte Solutions - Hofmeister Series Effects

Author(s):

R.A. Curtis, J. Ulrich, J.M. Prausnitz, H.W. Blanch
Conference/Journal:

Biotechnology and Bioengineering, vol. 79, no. 4, pp. 367-380
Abstract:

Protein-protein interactions were measured for ovalbumin and for lysozyme in aqueous salt solutions. Protein-protein interactions are correlated with a proposed potential of mean force equal to the free energy to desolvate the protein surface that is made inaccessible to the solvent due to the protein-protein interaction. This energy is calculated from the surface free energy of the protein that is determined from the protein-salt preferential-interaction parameter measurements. In classical salting-out behavior, the protein-salt preferential interaction is unfavorable. Because addition of salt raises the surface free energy of the protein according to the surface-tension increment of the salt, protein-protein attraction increases, leading to a reduction in solubility. When the surface chemistry of proteins is altered by binding a specific ion, salting-in is obeserved when the interactions between (kosmotrope) ion-protein complexes are more repulsive than those between the uncomplexed proteins. However, salting-out is observed when interactions between (chaotrope) ion-protein complexes are more attractive than those of the uncomplexed proteins.

Further Information
Year:

2002
Type of Publication:

(01)Article
Supervisor:



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% Autogenerated BibTeX entry
@Article { CurEtal:2002:IFA_823,
    author={R.A. Curtis and J. Ulrich and J.M. Prausnitz and H.W. Blanch},
    title={{Protein-Protein Interactions in Concentrated Electrolyte
	  Solutions - Hofmeister Series Effects}},
    journal={Biotechnology and Bioengineering},
    year={2002},
    volume={79},
    number={4},
    pages={367--380},
    month=aug,
    url={http://control.ee.ethz.ch/index.cgi?page=publications;action=details;id=823}
}
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