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Probing the urea dependence of residual structure in denatured human α-lactalbumin

Abstract:

Backbone 15N relaxation parameters and 15N-1NN residual dipolar couplings (RDCs) have been measured for a variant of human α-lactalbumin (α-LA) in 4, 6, 8 and 10 M urea. In the α-LA variant, the eight cysteine residues in the protein have been replaced by alanines (all-Ala α-LA). This protein is a partially folded molten globule at pH 2 and has been shown previously to unfold in a stepwise non-cooperative manner on the addition of urea. 15

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Publication status:
Published
Peer review status:
Peer reviewed
Version:
Publisher's version

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Publisher copy:
10.1007/s10858-009-9342-y

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Institution:
University of Oxford
Department:
Mathematical,Physical & Life Sciences Division - Chemistry - Inorganic Chemistry Laboratory
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Institution:
University of Oxford
Department:
Medical Sciences Division - Biochemistry
More by this author
Institution:
University of Oxford
Department:
Mathematical,Physical & Life Sciences Division - Chemistry - Inorganic Chemistry Laboratory
More by this author
Institution:
University of Oxford
Department:
Mathematical,Physical & Life Sciences Division - Chemistry - Inorganic Chemistry Laboratory
More by this author
Institution:
University of Oxford
Department:
Medical Sciences Division - Biochemistry
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Publisher:
Springer Publisher's website
Journal:
Journal of Biomolecular NMR Journal website
Volume:
45
Issue:
1-2
Pages:
121-131
Publication date:
2009
DOI:
EISSN:
1573-5001
ISSN:
0925-2738
URN:
uuid:1a37dfff-c48b-415a-8b74-aecb33bf29a1
Local pid:
ora:5469
Language:
English
Subjects:

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