Hemoglobin conformation(the T to R transition of hemoglobin) - Article Example

Hemoglobin conformation (the T to R transition of hemoglobin) Hemoglobin is a tetra metric protein and usually found in high concentrations in the red blood cells. They are responsible for transporting and binding oxygen in the body. Every hemoglobin consists up of four subunits two of which are alpha subunits and the other two are beta subunits. Each of the subunits there is capable of binding to an oxygen molecule via the heme group. Studies have shown that hemoglobin exists in one of the following conformations T (taut) and R (relaxed).

When the hemoglobin is deoxygenated (blue in color), it is found in the T state. The oxygenated hemoglobin (red) mostly triggers the interchanging to the R state. In the state of (T), the iron atom becomes planar with respect to the rest of the heme group this pulls the histamine, thus causing the larger scale structural change in the protein. Hemoglobin can be termed as a tetramer that makes up of two alpha-beta dimmers. The T to R transition requires that at least the hemoglobin subunits need to be bounded by oxygen.

Hemoglobin in the T state has low affinity for oxygen, the change in conformational can only occur under high concentrations of oxygen. In R state, the hemoglobin binds to oxygen with high affinity, thus leading to the deoxygenated subunits binding to oxygen. The red blood cells that are rich in oxygen are found in the lungs need to flow all over the body to supply the tissues with oxygen for the metabolic processes. The fundamental allosteric effectors of hemoglobin are the protons. At an extremely low PH, hemoglobin has lower affinity for oxygen than it does at the higher PHs.

In the present suggestions are made to changes in the stabilization free energy to specific amino acids residues in the interfaces of T to R transition.Work citedMihaela-Rita Mihailescu &Irina M. Russu. A signature of the T 3 R transition in Human hemoglobin, Lexington: Brandeis University.2001. http://www.pnas.org/content/98/7/3773.full.pdf+html. retrieved on 12/ 10/2012.