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Cover Picture: Chemically Programmed Supramolecular Assembly of Hemoprotein and Streptavidin with Alternating Alignment (Angew. Chem. Int. Ed. 16/2012)
Author(s) -
Oohora Koji,
Burazerovic Sabina,
Onoda Akira,
Wilson Yvonne M.,
Ward Thomas R.,
Hayashi Takashi
Publication year - 2012
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201201226
Subject(s) - streptavidin , linker , myoglobin , supramolecular chemistry , moiety , hemeprotein , supramolecular assembly , chemistry , heme , dimer , crystallography , stereochemistry , biotin , biochemistry , organic chemistry , crystal structure , computer science , enzyme , operating system
An alternating protein assembly of myoglobin dimer (green) and streptavidin (gray) was made by using a synthesized cofactor dyad, which has a flexible linker between a heme moiety (red) and a bis(biotin) unit (blue). The specific interactions between the three components resulted in formation of a supramolecular submicrometer‐sized fibrous assembly, which was characterized by AFM, as reported by T. Hayashi, T. R. Ward, and co‐workers in their Communication on page 3818 ff.