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 In the α-LA variant, the eight cysteine residues in the protein have been replaced by alanines (all-Ala α-LA).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. 15Expand abstract
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- V. A. Higman et al.
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- Citation: Higman, V. A. et al. (2009). 'Probing the urea dependence of residual structure in denatured human α-lactalbumin', Journal of Biomolecular NMR 45(1-2), 121-131 [Available at http://www.springer.com/physics/biophysics+%26+biological+physics/journal/10858]. © the authors 2009. This article is distributed under the terms of the Creative Commons Attribution Noncommercial License which permits any noncommercial use, distribution, and reproduction in any medium, provided the original authors and source are credited.
Probing the urea dependence of residual structure in denatured human α-lactalbumin
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