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000017773 1001_ $$0P:(DE-Juel1)VDB86654$$aHeinen, M.$$b0$$uFZJ
000017773 245__ $$aViscosity and diffusion: crowding and salt effects in protein solutions
000017773 260__ $$aCambridge$$bRoyal Society of Chemistry (RSC)$$c2012
000017773 300__ $$a1404-1419
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000017773 520__ $$aWe report on a joint experimental–theoretical study of collective diffusion in, and static shear viscosity of solutions of bovine serum albumin (BSA) proteins, focusing on the dependence on protein and salt concentration. Data obtained from dynamic light scattering and rheometric measurements are compared to theoretical calculations based on an analytically treatable spheroid model of BSA with isotropic screened Coulomb plus hard-sphere interactions. The only input to the dynamics calculations is the static structure factor obtained from a consistent theoretical fit to a concentration series of small-angle X-ray scattering (SAXS) data. This fit is based on an integral equation scheme that combines high accuracy with low computational cost. All experimentally probed dynamic and static properties are reproduced theoretically with an at least semi-quantitative accuracy. For lower protein concentration and low salinity, both theory and experiment show a maximum in the reduced viscosity, caused by the electrostatic repulsion of proteins. On employing our theoretical and experimental results, the applicability range of a generalized Stokes–Einstein (GSE) relation connecting viscosity, collective diffusion coefficient, and osmotic compressibility, proposed by Kholodenko and Douglas [Phys. Rev. E, 1995, 51, 1081] is examined. Significant violation of the GSE relation is found, both in experimental data and in theoretical models, in concentrated systems at physiological salinity, and under low-salt conditions for arbitrary protein concentrations.
000017773 536__ $$0G:(DE-Juel1)FUEK505$$2G:(DE-HGF)$$aBioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung$$cP45$$x0
000017773 7001_ $$0P:(DE-HGF)0$$aZanini, F.$$b1
000017773 7001_ $$0P:(DE-HGF)0$$aRoosen-Runge, F.$$b2
000017773 7001_ $$0P:(DE-HGF)0$$aFedunová, D.$$b3
000017773 7001_ $$0P:(DE-HGF)0$$aZhang, F.$$b4
000017773 7001_ $$0P:(DE-HGF)0$$aHennig, M.$$b5
000017773 7001_ $$0P:(DE-HGF)0$$aSeydel, T.$$b6
000017773 7001_ $$0P:(DE-HGF)0$$aSchweins, R.$$b7
000017773 7001_ $$0P:(DE-HGF)0$$aSztucki, M.$$b8
000017773 7001_ $$0P:(DE-HGF)0$$aAntalik, M.$$b9
000017773 7001_ $$0P:(DE-HGF)0$$aSchreiber, F.$$b10
000017773 7001_ $$0P:(DE-Juel1)130858$$aNägele, G.$$b11$$uFZJ
000017773 773__ $$0PERI:(DE-600)2191476-X$$a10.1039/c1sm06242e$$gVol. 8$$n5$$p1404-1419$$tSoft matter$$v8$$x1744-683X$$y2012
000017773 8567_ $$uhttp://dx.doi.org/10.1039/c1sm06242e
000017773 8564_ $$uhttps://juser.fz-juelich.de/record/17773/files/4632.pdf$$yOpenAccess
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