| Literature DB >> 23929823 |
Zehavit Dadon1, Manickasundaram Samiappan, Anat Shahar, Raz Zarivach, Gonen Ashkenasy.
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.Entities:
Keywords: coiled coils; depsipeptides; dynamic chemistry; peptide networks; thiodepsipeptides
Mesh:
Substances:
Year: 2013 PMID: 23929823 DOI: 10.1002/anie.201303900
Source DB: PubMed Journal: Angew Chem Int Ed Engl ISSN: 1433-7851 Impact factor: 15.336