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Rapid collapse and slow structural reorganisation during the refolding of bovine alpha-lactalbumin.

Abstract:

The refolding of bovine alpha-lactalbumin (BLA) from its chemically denatured state in 6 M GuHCl has been investigated by a variety of complementary biophysical approaches. CD experiments indicate that the species formed in the early stages of refolding of the apo-protein have at least 85 % of the alpha-helical content of the native state, and kinetic NMR experiments show that they possess near-native compactness. Hydrogen exchange measurements using mass spectrometry and NMR indicate that pe...

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Publication status:
Published

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Publisher copy:
10.1006/jmbi.1999.2687

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Journal:
Journal of molecular biology
Volume:
288
Issue:
4
Pages:
673-688
Publication date:
1999-05-05
DOI:
EISSN:
1089-8638
ISSN:
0022-2836
URN:
uuid:48a9ee6a-ae65-4872-8849-b296e77761f7
Source identifiers:
59216
Local pid:
pubs:59216

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