Virial Expansions for Low Dimensional Ferrofluids

1991 ◽  
Vol 248 ◽  
Author(s):  
M. Widom ◽  
H. Zhang
Keyword(s):  
Magnetic Susceptibility ◽  
Magnetic Particles ◽  
Particle Density ◽  
Hard Spheres ◽  
Three Dimensional ◽  
Virial Coefficients ◽  
Colloidal Suspensions ◽  
Second Virial Coefficients ◽  
Dilute Gas ◽  
Low Dimensional

AbstractFerrofluids are colloidal suspensions of magnetic particles which we model as a dilute gas of dipolar hard spheres. At low particle density the osmotic pressure and magnetic susceptibility may be expanded in a virial series. We evaluate the second virial coefficients for fluids confined to a line, or to a plane, as well as ordinary three dimensional fluids in ellipsoidal containers. We focus our attention on anisotropy of the magnetic susceptibility and point out the role of particle chaining in determining the magnetic anisotropy of low dimensional ferrofluids.

Exchange and Direct Second Virial Coefficients for Hard Spheres

1966 ◽  
Vol 45 (2) ◽  
pp. 499-508 ◽  
Author(s):  
Marjorie E. Boyd ◽  
Sigurd Yves Larsen ◽  
John E. Kilpatrick
Keyword(s):  
Hard Spheres ◽  
Virial Coefficients ◽  
Second Virial Coefficients

Second virial coefficients of dipolar hard spheres

2010 ◽  
Vol 22 (32) ◽  
pp. 325104 ◽  
Author(s):  
Albert P Philipse ◽  
Bonny W M Kuipers
Keyword(s):  
Hard Spheres ◽  
Virial Coefficients ◽  
Second Virial Coefficients

Erratum: ``Exchange and Direct Second Virial Coefficients for Hard Spheres''

1967 ◽  
Vol 46 (3) ◽  
pp. 1224-1224 ◽  
Author(s):  
Marjorie E. Boyd ◽  
Sigurd Yves Larsen ◽  
John E. Kilpatrick
Keyword(s):  
Hard Spheres ◽  
Virial Coefficients ◽  
Second Virial Coefficients

scholarly journals Protein aggregation in salt solutions

2015 ◽  
Vol 112 (21) ◽  
pp. 6766-6770 ◽  
Author(s):  
Miha Kastelic ◽  
Yurij V. Kalyuzhnyi ◽  
Barbara Hribar-Lee ◽  
Ken A. Dill ◽  
Vojko Vlachy
Keyword(s):  
Protein Aggregation ◽  
Hard Spheres ◽  
Protein Crystallization ◽  
Virial Coefficients ◽  
Necessary Condition ◽  
Thermodynamic Perturbation Theory ◽  
Salt Solutions ◽  
Biological Drugs ◽  
Second Virial Coefficients ◽  
Square Well

Protein aggregation is broadly important in diseases and in formulations of biological drugs. Here, we develop a theoretical model for reversible protein–protein aggregation in salt solutions. We treat proteins as hard spheres having square-well-energy binding sites, using Wertheim’s thermodynamic perturbation theory. The necessary condition required for such modeling to be realistic is that proteins in solution during the experiment remain in their compact form. Within this limitation our model gives accurate liquid–liquid coexistence curves for lysozyme and γ IIIa-crystallin solutions in respective buffers. It provides good fits to the cloud-point curves of lysozyme in buffer–salt mixtures as a function of the type and concentration of salt. It than predicts full coexistence curves, osmotic compressibilities, and second virial coefficients under such conditions. This treatment may also be relevant to protein crystallization.

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