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

Abstract:

Backbone (15)N relaxation parameters and (15)N-(1)H(N) residual dipolar couplings (RDCs) have been measured for a variant of human alpha-lactalbumin (alpha-LA) in 4, 6, 8 and 10 M urea. In the alpha-LA variant, the eight cysteine residues in the protein have been replaced by alanines (all-Ala alpha-LA).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)N R(2) values in some region...

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Publication status:
Published

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

Authors


Higman, VA More by this author
Rösner, HI More by this author
Ugolini, R More by this author
Greene, LH More by this author
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Institution:
University of Oxford
Department:
Oxford, MSD, Biochemistry
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Journal:
Journal of biomolecular NMR
Volume:
45
Issue:
1-2
Pages:
121-131
Publication date:
2009-09-05
DOI:
EISSN:
1573-5001
ISSN:
0925-2738
URN:
uuid:38a35512-374c-4788-b583-d2bf73bf27c8
Source identifiers:
34801
Local pid:
pubs:34801

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