Protein interactions studied by SAXS: effect of ionic strength and protein concentration for BSA in aqueous solutions.
We have studied a series of samples of bovine serum albumin (BSA) solutions with protein concentration, c, ranging from 2 to 500 mg/mL and ionic strength, I, from 0 to 2 M by small-angle X-ray scattering (SAXS). The scattering intensity distribution was compared to simulations using an oblate ellips...
Main Authors: | Zhang, F, Skoda, M, Jacobs, R, Martin, R, Martin, C, Schreiber, F |
---|---|
Format: | Journal article |
Language: | English |
Published: |
2007
|
Similar Items
-
Protein-protein interactions in ovalbumin solutions studied by small-angle scattering: effect of ionic strength and the chemical nature of cations.
by: Ianeselli, L, et al.
Published: (2010) -
Dynamics of highly concentrated protein solutions around the denaturing transition
by: Hennig, M, et al.
Published: (2012) -
Dynamics of highly concentrated protein solutions around the denaturing transition
by: Hennig, M, et al.
Published: (2012) -
Hydration and interactions in protein solutions containing concentrated electrolytes studied by small-angle scattering.
by: Zhang, F, et al.
Published: (2012) -
Hydration and interactions in protein solutions containing concentrated electrolytes studied by small-angle scattering
by: Zhang, F, et al.
Published: (2012)