Front Cover: Construction of a Triangle‐Shaped Trimer and a Tetrahedron Using an α‐Helix‐Inserted Circular Permutant of Cytochrome c₅₅₅ (Chem. Asian J. 10/2018)

Abstract

A building block protein BBP is designed by circularly permutating thermostable cytochrome c555 (pictured as pink and green pieces on the front cover) and connecting the original N‐ and C‐terminal α‐helices with an α‐helical linker (blue piece). The N‐terminal α‐helix of one BBP molecule interacts intermolecularly with the C‐terminal α‐helix of another BBP molecule in a defined angle, resulting in the formation of a triangle‐shaped trimer and a tetrahedron by four of these trimers. This approach of combining circular permutation and an α‐helical linker insertion is promising for constructing organized protein structures. More information can be found in the https://doi.org/10.1002/asia.201800252