Hemoglobin Nylon Model
This nylon model is being discontinued as we redesign it for 3D printing in a larger size and a more durable material. Best of all, we believe we will be able to offer it at a lower price! Watch for its updated availability on our Facebook page, Instagram, and eNewsletter.
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.
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6.5'' nylon model is made on a rapid prototyping machine – not mass produced. It is more resilient than plaster models, but will break if abused.
* The value displayed refers to the "starting price".
