Abstract
Natural protein assemblies have encouraged scientists to create large supramolecular systems consisting of various protein motifs. In the case of hemoproteins containing heme as a cofactor, several approaches have been reported to form artificial assemblies with various structures such as fibers, sheets, networks, and cages. This chapter describes the design, preparation, and characterization of cage-like micellar assemblies for chemically modified hemoproteins including hydrophilic protein units attached to hydrophobic molecules. Detailed procedures are described for constructing specific systems using cytochrome b562 and hexameric tyrosine-coordinated heme protein as hemoprotein units with heme-azobenzene conjugate and poly-N-isopropylacrylamide as attached molecules.
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Acknowledgments
We acknowledge supports from JSPS KAKENHI JP15H05804, JP15K21707, JP20H00403, and JP20H02755.
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Oohora, K., Hayashi, T. (2023). Preparation of Cage-Like Micellar Assemblies of Engineered Hemoproteins. In: Ueno, T., Lim, S., Xia, K. (eds) Protein Cages. Methods in Molecular Biology, vol 2671. Humana, New York, NY. https://doi.org/10.1007/978-1-0716-3222-2_5
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DOI: https://doi.org/10.1007/978-1-0716-3222-2_5
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