Laboratory for Systems Chemistry
Prof. Gonen Ashkenasy Research Group
A high-resolution structure that provides insight into coiled-coil thiodepsipeptide dynamic chemistry
Stable and reactive: A crystal structure at 1.35Å of a thioester coiled-coil protein reveals high similarity to all-peptide-bond proteins. In these assemblies, the thioester bonds are kept reactive towards thiol molecules in the mixture. This enables efficient domain exchange between proteins in response to changes in folding conditions or introduction of external templates.
| Publication language | English |
| Pages | 9944-9947 |
| Volume | 52 |
| Issue number | 38 |
| Publication status | Published - 16.09.2013 |
Keywords
coiled coils
depsipeptides
dynamic chemistry
peptide networks
thiodepsipeptides
ASJC Scopus subject areas
Catalysis
General Chemistry
