Department of Chemistry, Ben Gurion University of the Negev, Beer Sheva, 84105 (Israel).
Angew Chem Int Ed Engl. 2013 Sep 16;52(38):9944-7. doi: 10.1002/anie.201303900. Epub 2013 Aug 8.
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.
硫酯卷曲螺旋蛋白在 1.35 Å 处的晶体结构显示出与全肽键蛋白的高度相似性。在这些组装体中，硫酯键对混合物中的硫醇分子保持反应性。这使得蛋白质在折叠条件变化或引入外部模板时能够有效地进行结构域交换。
