Our hemoglobin nylon model is the 3-D protein
structure that every science classroom needs to explore the quaternary
structure of proteins. It also features the ß-globin protein mutation
that causes sickle cell anemia.
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.
This 6.5'' alpha carbon backbone nylon model is made on a rapid
prototyping machine – not mass produced. It is more resilient than
plaster models, but will break if abused. Its PDB file is 1A3N.pdb.