Note: Please use the scroll bar to see the entire link.
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
developed is
![]() |
||
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.
|