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Viscosity and Diffusion: Crowding and Salt Effects in Protein Solutions | | Marco Heinen
; Fabio Zanini
; Felix Roosen-Runge
; Diana Fedunová
; Fajun Zhang
; Marcus Hennig
; Tilo Seydel
; Ralf Schweins
; Michael Sztucki
; Marián Antalík
; Frank Schreiber
; Gerhard Nägele
; | | Date: |
14 Sep 2011 | | Abstract: | We 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. The validity range of a generalized
Stokes-Einstein (GSE) relation connecting viscosity, collective diffusion
coefficient, and osmotic compressibility, proposed by Kholodenko and Douglas
[PRE 51, 1081 (1995)] is examined. Significant violation of the GSE relation is
found, both in experimental data and in theoretical models, in semi-dilute
systems at physiological salinity, and under low-salt conditions for arbitrary
protein concentrations. | | Source: | arXiv, 1109.3101 | | Services: | Forum | Review | PDF | Favorites | |
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