Heike I. Rösner

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Structural investigations of molten globules provide an important contribution towards understanding protein folding pathways. A close similarity between equilibrium molten globule states and kinetic species observed during refolding has been reported for several proteins. However, the experimental conditions, and in particular the pH, under which the(More)
Backbone N relaxation parameters and N–H residual dipolar couplings (RDCs) have been measured for a variant of human a-lactalbumin (a-LA) in 4, 6, 8 and 10 M urea. In the a-LA variant, the eight cysteine residues in the protein have been replaced by alanines (all-Ala a-LA). This protein is a partially folded molten globule at pH 2 and has been shown(More)
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 In the alpha-LA variant, the eight cysteine residues in the protein have been replaced by alanines (all-Ala alpha-LA).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(More)
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