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Local and global cooperativity in the human alpha-lactalbumin molten globule.

Abstract:

NMR spectroscopy has been used to follow the urea-induced unfolding of the low pH molten globule states of a single-disulfide variant of human alpha-lactalbumin ([28-111] alpha-LA) and of two mutants, each with a single proline substitution in a helix. [28-111] alpha-LA forms a molten globule very similar to that formed by the wild-type four-disulfide protein, and this variant has been used as a model for the alpha-lactalbumin (alpha-LA) molten globule in a number of studies. The urea-induced...

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Publication status:
Published

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Publisher copy:
10.1016/j.jmb.2004.02.045

Authors


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Institution:
University of Oxford
Division:
MSD
Department:
Biochemistry
Role:
Author
Journal:
Journal of molecular biology
Volume:
338
Issue:
1
Pages:
149-158
Publication date:
2004-04-01
DOI:
EISSN:
1089-8638
ISSN:
0022-2836
Source identifiers:
99778
Language:
English
Keywords:
Pubs id:
pubs:99778
UUID:
uuid:c467ffe7-3112-43f5-9887-aa0e3965fb03
Local pid:
pubs:99778
Deposit date:
2012-12-19

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