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Front Cover: Construction of a Triangle‐Shaped Trimer and a Tetrahedron Using an α‐Helix‐Inserted Circular Permutant of Cytochrome c 555 (Chem. Asian J. 10/2018)
Author(s) -
Oda Akiya,
Nagao Satoshi,
Yamanaka Masaru,
Ueda Ikki,
Watanabe Hiroki,
Uchihashi Takayuki,
Shibata Naoki,
Higuchi Yoshiki,
Hirota Shun
Publication year - 2018
Publication title -
chemistry – an asian journal
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.18
H-Index - 106
eISSN - 1861-471X
pISSN - 1861-4728
DOI - 10.1002/asia.201800587
Subject(s) - trimer , tetrahedron , helix (gastropod) , linker , terminal (telecommunication) , crystallography , molecule , cover (algebra) , combinatorics , chemistry , physics , dimer , stereochemistry , computer science , mathematics , biology , engineering , quantum mechanics , mechanical engineering , ecology , telecommunications , organic chemistry , snail , operating system
A building block protein BBP is designed by circularly permutating thermostable cytochrome c 555 (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 Communication by Shun Hirota et^^al. on page 964 in Issue 8, 2018