Structure of ferritin molecule. (a) Appearance of ferritin and (b) Cross section model of ferritin core. The spherical hollow shell is composed of 24 polypeptide subunits. The inner and outer diameters of the protein shell are about 7 nm and 13 nm, respectively. The self-assembled protein cage has the ability to sequester and store iron as hydrated iron oxide in the internal cavity.
Two-dimensional ferritin crystal array with field emission type high resolution SEM. The white dots represent ferritin cores. The outer protein shell was removed by UV ozone treatment. The ferritin molecule densities of the core were approximately (a) , (b) , and (c) , respectively.
Difference in amounts of ferritin adsorbed between hydrophilic and hydrophobic substrate surfaces. (a) Hydrophilic, (b) slightly hydrophilic, (c) slightly hydrophobic, and (d) coexisting hydrophilic and hydrophobic areas. The dots were arranged randomly. Some dots gathered to form clusters, and some dots were isolated.
Machining of ferritin protein molecule in pure water using a conventional AFM. (a) Before machining and (b) after machining with a force of 700 nN.
Dynamic images of ferritin molecule-substrate interaction in pure water by high-speed AFM. (a) First image before adding ferritin solution. [(b)–(n)] Dynamic images of ferritin molecules after adding ferritin solution. The arrows from (b) to (n) show the same molecule of ferritin. (o) High-speed AFM image of a ferritin indicated by the arrow in figure and (p) cross-sectional profile of (o).
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