Hemoglobin transports oxygen through the blood. This quaternary protein complex is made up of 4 subunits: 2 α-chains and 2 β-chains. One of the ß-chains on our 3-D protein model is magnet-docked so it can be removed for closer examination. The heme group and its oxygen on the removable ß-globin are also magnet-docked. The glutamic acid side chain at position 6 of the ß-globin chain can be exchanged for a valine side chain – representing the change in the ß-globin protein that leads to sickle cell anemia. The model can be used to discuss quaternary structure, blood physiology, and the lasting effects of a single amino acid mutation on a protein.
The 1962 Nobel Prize in Chemistry was awarded jointly to Max Ferdinand Perutz and John Cowdery Kendrew "for their studies of the structures of globular proteins". Max Ferdinand Perutz solved the structure of hemoglobin in 1959.