Add to ORKGTn recent publications it was pointed out that there is a correlation between the observed values of the solubility of proteins in aqueous solutions and the second virial coefficient of the solution. In this paper we give a theoretical explanation of this relation. The derived theoretical expression describes the experimentally observed relation between solubility and virial coefficient quite accurately. It is concluded that a variation of the crystallization conditions has little effect on the anisotropy or the range of the interactions between the protein molecules. Analysis of the data for lysozyme indicates a strong anisotropy of the interactions between the molecules.</p
We study theoretically thermodynamic properties of spherical globular proteins in aqueous solution w...
We quantitatively link the macroscopic phase behavior of protein solutions to protein–protein intera...
AbstractThe osmotic second virial coefficient, B2, obtained by light scattering from protein solutio...
Tn recent publications it was pointed out that there is a correlation between the observed values of...
The osmotic second virial coefficient, B, is a dilute solution parameter, so one may wonder what rel...
The relationship of second virial coefficient, B22 with solubility is reviewed and its relationship ...
A molecular basis is presented for characterizing the osmotic second virial coeƒcient, B 22, of dilu...
135 p.Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 1998.Protein interactions in solut...
AbstractThe thermodynamic properties of protein solutions are determined by the molecular interactio...
In this work, osmotic second virial coefficients (B22) were determined and correlated with the measu...
International audienceInterparticle lysozyme interactions in solution have been studied by small ang...
There is a strong link between solubility, and thus crystallisation, and the molecular interactions ...
Experimental data for ovalbumin and lysozyme are presented to highlight the nonequivalence of second...
A negative second virial coefficient has long been a predictor of potential protein crystallization ...
A chromatographic method is used to measure interactions between dissimilar proteins in aqueous elec...
We study theoretically thermodynamic properties of spherical globular proteins in aqueous solution w...
We quantitatively link the macroscopic phase behavior of protein solutions to protein–protein intera...
AbstractThe osmotic second virial coefficient, B2, obtained by light scattering from protein solutio...
Tn recent publications it was pointed out that there is a correlation between the observed values of...
The osmotic second virial coefficient, B, is a dilute solution parameter, so one may wonder what rel...
The relationship of second virial coefficient, B22 with solubility is reviewed and its relationship ...
A molecular basis is presented for characterizing the osmotic second virial coeƒcient, B 22, of dilu...
135 p.Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 1998.Protein interactions in solut...
AbstractThe thermodynamic properties of protein solutions are determined by the molecular interactio...
In this work, osmotic second virial coefficients (B22) were determined and correlated with the measu...
International audienceInterparticle lysozyme interactions in solution have been studied by small ang...
There is a strong link between solubility, and thus crystallisation, and the molecular interactions ...
Experimental data for ovalbumin and lysozyme are presented to highlight the nonequivalence of second...
A negative second virial coefficient has long been a predictor of potential protein crystallization ...
A chromatographic method is used to measure interactions between dissimilar proteins in aqueous elec...
We study theoretically thermodynamic properties of spherical globular proteins in aqueous solution w...
We quantitatively link the macroscopic phase behavior of protein solutions to protein–protein intera...
AbstractThe osmotic second virial coefficient, B2, obtained by light scattering from protein solutio...