- 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 In the alpha-LA variant, the eight cysteine residues in the protein have been replaced by alanines (all-Ala alpha-LA).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...
Expand abstract - Publication status:
- Published
- Publisher copy:
- 10.1007/s10858-009-9342-y
-
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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
- Copyright date:
- 2009
Journal article
Probing the urea dependence of residual structure in denatured human alpha-lactalbumin.
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