A high-resolution structure that provides insight into coiled-coil thiodepsipeptide dynamic chemistry

Abstract

Stable and reactive: A crystal structure at 1.35 Å 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.

Keywords: coiled coils; depsipeptides; dynamic chemistry; peptide networks; thiodepsipeptides.