Sandbox GGC8

DEOXY HUMAN HEMOGLOBIN A

spinqualitylabelsall models Caption for this structure Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D <scene name='78/781194/Deoxy_human_hemoglobin_a/1'>TextToBeDisplayed</scene> Function Hemoglobin A is an oxygen-transport protein. Hemoglobin is also an allosteric protein. It is a tetrameter composed of two types of sub units designated α and β, with stoichiometry α2β2 The function of Hemoglobin is to carry oxygen from the lungs to the other parts of the body . Hemoglobin also help to carry carbon dioxide through the blood cells.Hemoglobin A which is a component of the red blood cells also help with the transportation of carbon dioxide and hydrogen ions to the lungs. Hemoglobin proteins are capable of carrying four molecules of Oxygen . Hemoglobin also help red blood cells to maintain their disc like shape , which allows them to move freely through the blood vessels. Each sub-unit of Hemoglobin A contains a heme prosthetic group. The heme molecules give hemoglobin its red color. 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 Most of the understanding that of human physiology and pathology come from laboratory research that were performed on Hemoglobin. Structural highlights This scene show the relative orientation of the proximal His87 and the distal His 58 This scene show the structure of the full hemoglobin this scene show the proximal 92 His and distal 63 His You may include any references to papers as in: the use of JSmol in Proteopedia or to the article describing Jmol to the rescue. The first structure is a ball stick representing the approximate distance distance between two His 87 proximal and His distal 58 from the hemoglobin structure. The second scene consist of a full sturcture of the hemoglobin and all of its components. The third scene is From the Beta chain of the hemoglobin it is showing the distance from the proximal His 92 to the distal His 63 . This is a sample scene created with SAT to color by Group, and another to make a transparent representation of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

References

Crystal structure of Lysβ182-Lysβ282 crosslinked hemoglobin: A possible allosteric intermediate1 https://www.sciencedirect.com/science/article/pii/S0022283600935253?via%3Dihub#FIG4