Abstract
Small angle neutron scattering study reveals that at pD ≈ 7.0, above the isoelectric point of the globular protein Bovine Serum Albumin (BSA), in the presence of different divalent ions (Mg2+, Ca2+, Sr2+ and Ba2+), the short-range attractive interaction remains nearly constant and the intermediate-range repulsive interaction decreases with increasing salt concentration up to a certain concentration value but after that remains unchanged. However, for the monovalent ion (Na+), repulsive interaction decreases gradually up to 1 M salt concentration. Dynamic light scattering study shows that for all ions, diffusion coefficient of BSA decreases with increasing salt concentration and then nearly saturates.
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