Title : Reversible unfolding of bovine beta-lactoglobulin mutants without a free thiol group.

Pub. Date : 2003 Nov 21

PMID : 12963719






2 Functional Relationships(s)
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1 These results indicate that intramolecular and intermolecular thiol-disulfide exchange reactions cause the low reversibility of wild-type beta-lg especially at neutral pH and that the mutation of Cys-121 improves the reversibility, enabling us to study the folding of beta-lg more exactly under various conditions. Cysteine beta-lactoglobulin Bos taurus
2 These results indicate that intramolecular and intermolecular thiol-disulfide exchange reactions cause the low reversibility of wild-type beta-lg especially at neutral pH and that the mutation of Cys-121 improves the reversibility, enabling us to study the folding of beta-lg more exactly under various conditions. Cysteine beta-lactoglobulin Bos taurus