- Abstract:
-
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 ellipsoid form factor with radii of 17 x 42 x 42 A, combined with either a screened Coulomb, repulsive structure factor, SSC(q), or an attractive square-well structure factor, SSW(q). At pH = 7, BSA is n...
Expand abstract - Publication status:
- Published
- Publisher copy:
- 10.1021/jp0649955
-
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- Journal:
- The journal of physical chemistry. B
- Volume:
- 111
- Issue:
- 1
- Pages:
- 251-259
- Publication date:
- 2007-01-05
- DOI:
- EISSN:
-
1520-5207
- ISSN:
-
1520-6106
- URN:
-
uuid:56095f4a-3fdc-4823-a139-33ea3a26c9f9
- Source identifiers:
-
64712
- Local pid:
- pubs:64712
- Copyright date:
- 2007
Journal article
Protein interactions studied by SAXS: effect of ionic strength and protein concentration for BSA in aqueous solutions.
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