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In this experiment, the ferritin contains an iron-mineral core
Questions: In your experiment, what amount of iron did the ferritin sample contain? Was the sample saturated?
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Figure 1:This is a molecular model of the ferritin protein with a 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 ribbons 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. However, for a clearer view of the three-dimensionality, the mineral core is not shown to be connected to the protein shell in this picture. |
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
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Figure 1: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 the stick representation. |