Abstract
Abstract
Monellin is a protein with an intense sweet taste. It is known to consist of two dissimilar polypeptide chains that are tightly but noncovalently bound. Monellin is also known to contain a single sulfhydryl group; in native monellin it appears to be buried within the interior of the protein. An oligomer of monellin is demonstrated to form in the presence of protein denaturants. It appears to involve dimerization through formation of a disulfide linkage. Formation of larger aggregates, which occurs during removal of denaturant, is postulated to involve the molecular species [monellin]2 as an intermediate.
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