Ololade fatunmbi

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This interaction shields Hb residues that are prone to oxidative modification.
This interaction shields Hb residues that are prone to oxidative modification.
== Disease ==
== Disease ==
-
Intravascular hemolysis
+
 
 +
Intravascular hemolysis
 +
 
== Relevance ==
== Relevance ==

Revision as of 23:21, 20 November 2014

Contents

Haptoglobin-Hemoglobin Structure

Drag the structure with the mouse to rotate

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)


This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

</StructureSection>

References

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.

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Ololade Fatunmbi

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