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 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 of a specific ion, salting-in is observed 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.
journal_name
Biotechnol Bioengjournal_title
Biotechnology and bioengineeringauthors
Curtis RA,Ulrich J,Montaser A,Prausnitz JM,Blanch HWdoi
10.1002/bit.10342subject
Has Abstractpub_date
2002-08-20 00:00:00pages
367-80issue
4eissn
0006-3592issn
1097-0290journal_volume
79pub_type
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