Abstract
Targeted insertion of a non-native diselenide cross-link into a cysteine-rich protein can be exploited to direct the early stages of oxidative folding so as to avoid accumulation of unproductive intermediates that limit folding efficiency. This simple strategy could facilitate the production of many difficult-to-fold peptides and proteins.
| Original language | English |
|---|---|
| Pages (from-to) | 5585-5588 |
| Number of pages | 4 |
| Journal | Angewandte Chemie - International Edition |
| Volume | 51 |
| Issue number | 23 |
| DOIs | |
| State | Published - 4 Jun 2012 |
| Externally published | Yes |
Keywords
- diselenide bonds
- disulfide bonds
- oxidative folding
- selenocysteine
- thiol-disulfide exchange