Hemoglobin: Difference between revisions

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Eran Hodis, Joel L. Sussman, Marc Gillespie, Eric Martz, Jaime Prilusky, Alexander Berchansky, Karl Oberholser, Michal Harel, Ann Taylor, Mark Hoelzer, Karsten Theis, Tihitina Y Aytenfisu, Hannah Campbell

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	<scene name='Hemoglobin/Anchortrace/5'>Anchoring of the heme</scene> is facilitated by a histidine nitrogen that binds to the iron. A second histidine is near the bound oxygen. The "arms" (propanoate groups) of the heme are hydrophilic and face the surface of the protein while the hydrophobic portions of the heme are buried among the hydrophobic amino acids of the protein.		<scene name='Hemoglobin/Anchortrace/5'>Anchoring of the heme</scene> is facilitated by a histidine nitrogen that binds to the iron. A second histidine is near the bound oxygen. The "arms" (propanoate groups) of the heme are hydrophilic and face the surface of the protein while the hydrophobic portions of the heme are buried among the hydrophobic amino acids of the protein.

	Perhaps the most well-known disease caused by a mutation in the hemoglobin protein is sickle-cell anemia. It results from a mutation of the sixth residue in the β hemoglobin monomer from <scene name='32/32/Hemoglobins_1hho/9'>glutamic acid to a valine</scene>. This hemoglobin variant is termed 'hemoglobin S' ([[2hbs]]). See also [[Ann Taylor/Hemoglobin]].		Perhaps the most well-known disease caused by a mutation in the hemoglobin protein is sickle-cell anemia. It results from a mutation of the sixth residue in the β hemoglobin monomer from <scene name='32/32/Hemoglobins_1hho/9'>glutamic acid to a valine</scene>. This hemoglobin variant is termed 'hemoglobin S' ([[2hbs]]). See also [[Ann Taylor/Hemoglobin]] and [[Hemoglobin (Hebrew)]].