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...
| Автори: | , , , , , , |
|---|---|
| Формат: | Journal article |
| Мова: | English |
| Опубліковано: |
2003
|