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Surface properties are highly sensitive to small ph induced changes in the 3-D structure of alpha-lactalbumin.

Abstract:

The change in structure of bovine alpha-lactalbumin in environments of decreasing pH from pH 7 to pH 3 was followed using high-resolution NMR and hydrogen exchange studies. The effect of the changes in the structure on the surface properties of the protein was also measured. As the pH was decreased from pH 7 toward pH 2, at which alpha-lactalbumin adopts a molten globule state, a small but increasing proportion of the molecules in the sample partially unfold. There was on average a loss of te...

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Publication status:
Published

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Publisher copy:
10.1021/bi700999r

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Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Inorganic Chemistry
Role:
Author
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Journal:
Biochemistry
Volume:
47
Issue:
6
Pages:
1659-1666
Publication date:
2008-02-05
DOI:
EISSN:
1520-4995
ISSN:
0006-2960
URN:
uuid:e3ade765-5ba6-4a67-b726-d991535cc11e
Source identifiers:
40608
Local pid:
pubs:40608

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