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Protein interactions studied by SAXS: effect of ionic strength and protein concentration for BSA in aqueous solutions.

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...

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Publication status:
Published

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Publisher copy:
10.1021/jp0649955

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Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Physical and Theoretical Chem
Role:
Author
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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

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