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A simplified view of ligand binding and conformation energies in hemoglobin

A simplified view of ligand binding and conformation energies in hemoglobin
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Description: The deoxy (T) conformation is favored when no ligands are bound, due to the increased number of noncovalent interactions in the T state.

As YO2 increases (i.e., more ligands are bound) the energy provided by formation of the Fe-O2 bond stabilizes the R conformation relative to the T conformation.

The energetic cost of breaking stabilizing interactions in the deoxy state is paid by the formation of Fe-O2 bonds in the oxy state.

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Source: https://biology-forums.com/index.php?action=gallery;sa=view;id=34125
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