Sandbox GGC8
From Proteopedia
(Difference between revisions)
(This is the full Hemoglobin A structure) |
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- | == | + | ==Hemoglobin A== |
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene='78/781194/87_-58_his/1'> | <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene='78/781194/87_-58_his/1'> | ||
- | <scene name='78/781194/Deoxy_human_hemoglobin_a/1'><scene name='78/781194/Deoxy_human_hemoglobin_a/1'>TextToBeDisplayed</scene></scene> | ||
== Function == | == Function == | ||
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== Disease == | == Disease == | ||
- | + | The most well-known disease caused by a mutation in the hemoglobin A protein is sickle-cell anemia. Sickle-cell anemia results from a mutation of the sixth residue in the β hemoglobin monomer from glutamic acid to a valine. This hemoglobin variant is termed 'hemoglobin S' (2hbs). | |
== Relevance == | == Relevance == | ||
- | + | Most of the understanding that of human physiology and pathology come from laboratory research that were performed on Hemoglobin. | |
== Structural highlights == | == Structural highlights == |
Revision as of 15:04, 19 November 2019
Hemoglobin A
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References
Crystal structure of Lysβ182-Lysβ282 crosslinked hemoglobin: A possible allosteric intermediate1 https://www.sciencedirect.com/science/article/pii/S0022283600935253?via%3Dihub#FIG4
- ↑ 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
- ↑ 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