The Gluten Complex Studied by Urea Denaturation and Red-ox Titration
Gluten surface sites with low affinity for ANS, La low hydrophobicity, were more labile to urea than those with high hydrophobicity and disappeared nearly completely when urea was above 6 M. The surface of the gluten complex was only moderately affected by complete reduction, in which case less hydrophobic regions were more labile.
KeywordsUrea Titration Disulfide Tryptophan Macromolecule
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