Ololade fatunmbi

From Proteopedia

Revision as of 20:32, 21 November 2014

Haptoglobin-Hemoglobin Structure

Hemoglobin (Hb) is arguably one of the most studied proteins of all time. Hb is essential for life because for the oxygen transport in our bodies so that we can have energy. Like most entities in life, too much of something may actually harm you. High concentrations of Hb released from red blood cells could cost oxidative damage to the body. In order to prevent this, 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 and

Function

During intravascular hemolysis Hb which is physiological a is released from red blood cells in to the extracellular environment. Hb then dissociates into dimers exposing . Hp binds shields Hb and shields these redox active residues and exposes and epiptope recognized by the multifunctional receptor, CD163.

Structural highlights

What makes the binding between Hp so tight and nearly irreversible? The interaction between Hb and Hp is composed of various Hydrophobic and electrostatic interactions.

Disease

Intravascular hemolysis is implicated in various diseases

Relevance

(http://www.umass.edu)

My Research Interest

I am focused on structural elucidation of Hp and it's interact physiological partners through molecular modeling and native mass spectrometry.

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References

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