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Protein-protein interactions in ovalbumin solutions studied by small-angle scattering: effect of ionic strength and the chemical nature of cations.

Abstract:

The influence of ionic strength and of the chemical nature of cations on the protein-protein interactions in ovalbumin solution was studied using small-angle X-ray and neutron scattering (SAXS/SANS). The globular protein ovalbumin is found in dimeric form in solutions as suggested by SANS/SAXS experiments. Due to the negative charge of the proteins at neutral pH, the protein-protein interactions without any salt addition are dominated by electrostatic repulsion. A structure factor related to ...

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Publication status:
Published

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Publisher copy:
10.1021/jp9112156

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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:
114
Issue:
11
Pages:
3776-3783
Publication date:
2010-03-05
DOI:
EISSN:
1520-5207
ISSN:
1520-6106
URN:
uuid:39aa833b-df95-4c59-8195-995f901cbb07
Source identifiers:
298509
Local pid:
pubs:298509

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