作者: Tomomi Koshiyama , Naomi Kawaba , Tatsuo Hikage , Masanobu Shirai , Yuki Miura
DOI: 10.1021/BC9003052
关键词:
摘要: Protein assemblies have attracted increasing attention for construction of biohybrid materials. crystals can also be regarded as solid protein assemblies. The present work demonstrates that employed porous biomaterials by site-specific modifications the recombinant sperm whale myoglobin mutants. space group P6 provide hexagonal pores consisting building blocks six Mb molecules, which form a pore with diameter 40 A. On basis lattice structure crystals, we selected appropriate residues located on surface replacement cysteine. This enables modification via coupling maleimide derivatives. We succeeded in crystallizing modified mutants, retaining lattice, and consistently aligning nanosized functional molecules such fluorescein, eosin, Ru(bpy)3 into crystals. Our strategy ...