Protein-protein interactions in concentrated electrolyte solutions.

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 Bioeng

authors

Curtis RA,Ulrich J,Montaser A,Prausnitz JM,Blanch HW

doi

10.1002/bit.10342

subject

Has Abstract

pub_date

2002-08-20 00:00:00

pages

367-80

issue

4

eissn

0006-3592

issn

1097-0290

journal_volume

79

pub_type

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