Oxidative folding intermediates with nonnative disulfide bridges between adjacent cysteine residues.

The oxidative folding of the Amaranthus alpha-amylase inhibitor, a 32-residue cystine-knot protein with three disulfide bridges, was studied in vitro in terms of the disulfide content of the intermediate species. A nonnative vicinal disulfide bridge between cysteine residues 17 and 18 was found in t...

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מידע ביבליוגרפי
Main Authors: Cemazar, M, Zahariev, S, Lopez, J, Carugo, O, Jones, J, Hore, P, Pongor, S
פורמט: Journal article
שפה:English
יצא לאור: 2003