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Comparison of the structural and dynamical properties of holo and apo bovine alpha-lactalbumin by NMR spectroscopy.

Abstract:

In the presence of 0.5 M NaCl at pH 7.1, the Ca(2+)-free apo form of recombinant bovine alpha-lactalbumin (BLA) is sufficiently stabilised in its native state to give well-resolved NMR spectra at 20 degrees C. The (1)H and (15)N NMR resonances of native apo-BLA have been assigned, and the chemical-shifts compared with those of the native holo protein. Large changes observed between the two forms of BLA are mainly limited to the Ca(2+)-binding region of the protein. These data suggest that Na(...

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Publication status:
Published

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Publisher copy:
10.1006/jmbi.2001.4530

Authors


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Institution:
University of Oxford
Division:
MSD
Department:
Biochemistry
Role:
Author
Journal:
Journal of molecular biology More from this journal
Volume:
307
Issue:
3
Pages:
885-898
Publication date:
2001-03-01
DOI:
EISSN:
1089-8638
ISSN:
0022-2836
Language:
English
Keywords:
Pubs id:
pubs:100177
UUID:
uuid:d28cba53-3f45-4455-a852-e820bf8cf9ee
Local pid:
pubs:100177
Source identifiers:
100177
Deposit date:
2012-12-19

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