Interactive intermediates are formed during the urea unfolding of rhodanese.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference24 articles.
1. The enzyme rhodanese can be reactivated after denaturation in guanidinium chloride.
2. Low concentrations of guanidinium chloride expose apolar surfaces and cause differential perturbation in catalytic intermediates of rhodanese.
3. Detergent-assisted refolding of guanidinium chloride-denatured rhodanese. The effect of lauryl maltoside.
4. Detergent-assisted refolding of guanidinium chloride-denatured rhodanese. The effects of the concentration and type of detergent.
5. Micelle-assisted protein folding. Denatured rhodanese binding to cardiolipin-containing lauryl maltoside micelles results in slower refolding kinetics but greater enzyme reactivation.
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