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Contents 1 Haptoglobin-Hemoglobin Structure 2 Function 3 Disease 4 Relevance 5 Structural highlights 6 References

Haptoglobin-Hemoglobin Structure

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This is a default text for your page Ololade Fatunmbi. Click above on edit this page to modify. Be careful with the < and > signs. 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.

    Haptoglobin 1-1 (Hp), an abundant glycoprotein in blood binds free hemoglobin (Hb) dimers in one of the strongest non-covalent binding events known in biology. 

Function

This interaction shields Hb residues that are prone to oxidative modification.

Disease

Intravascular hemolysis

Relevance

Structural highlights

(http://www.umass.edu Igor)

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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