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In this experiment, the ferritin contains an iron-mineral core
Mineral Core Figure 1:
This is a molecular model of the ferritin protein with a CPK representation of the iron-mineral core. The view looks down the 4-fold channel at the mineral core. The subunits that comprise the 4-fold channel are represented as ribbons and the ribbons have the same color code as the subunits in Figure 1 in the main section of the tutorial. The rest of the subunits are shown in the stick representation. The iron-mineral core is depicted as rust-colored. This model shows only half of the ferritin shell. Recall that the mineral core is connected to the protein shell with covalent bonds to carboxylate residues.
Note: The mineral core is not shown to be connected to the protein shell in this picture, although the actual iron-mineral core is covalently bond to the carboxylate side chains in the protein wall.
Until recently, it was thought that all ferritin cores were
microcrystalline and identical. However, ferritin cores from a
variety of sources have now been studied using a variety of
experimental techniques (i.e., x-ray absorption spectroscopy,
Mossbauer spectroscopy, and high-resolution electron microscopy)
and a number of variations in the degree of structural and
magnetic ordering and level of hydration has been shown. One
simplified model compound of the iron-mineral core that has been
Mineral Core Figure 2:
This is a stick representation of the simplified model
compound for the iron-mineral core
Note: The carbon atoms are green, the hydrogens are white, the iron atoms are magenta, and the oxygen atoms are red in this stick representation.
Return To Iron-removal Process Section of Tutorial
Return To Compound-Structure Index