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You may include any references to papers as in: the use of JSmol in Proteopedia ^[1] or to the article describing Jmol ^[2] to the rescue.

Function

Hemoglobin can carry oxygen. It resides in red blood cells which use it to carry oxygen around the bodies of vertebrates. It is also what causes their blood to appear red.

Structural Highlights

Hemoglobin is made of four protein chains. Each chain looks like myoglobin, which is used to store oxygen in muscles. Each individual chain has a that has an iron atom that allows oxygen to bind. Of the chains, two are beta chains and two are alpha chains.

In the chain, the heme group has iron that allows the oxygen to bind.

Diseases

Sickle Cell Anemia

For the most part, amino acid sequences can be slightly different, but sometimes a change in the sequence can have a large impact. For example, in sickle cell anemia, glutamate 6 in the beta chain is mutated to valine, resulting in a structural change that allows hemoglobin to stick to each other and create stiff fibers, which creates the sickle shape in blood cells. These fibers are helpful because the malaria virus cannot live in blood cells with them, but can also lead to rupture of the blood cell, causing a loss of hemoglobin.

Thalassemia

This is another genetic disease involving hemoglobin. Here, there is some sort of error in the production of beta proteins. In normal hemoglobin, there is two alpha proteins and two beta, but when thalassemia occurs, there may be low levels or no beta proteins, decreasing the amount of functional hemoglobin and therefore supplies of red blood cells, often causing anemia.

Relevance

References

1. ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
2. ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644