π‘ Hemoglobin is a protein composed of a non-protein portion called a prosthetic group and a protein portion called globin.
π The structure of hemoglobin consists of four pyrrole rings with methyl and vinyl substituents, connected by metal bridges.
π¬ The iron molecule in hemoglobin forms six coordination bonds, including one with oxygen.
π Hemoglobin is a protein that plays a crucial role in carrying oxygen in the blood.
𧬠The structure of hemoglobin consists of four polypeptide chains: two alpha chains and two beta chains.
π§ The secondary structure of hemoglobin is mainly composed of alpha helices, which protect the iron from oxidation.
π The structure of hemoglobin consists of alpha helices and beta sheets.
𧬠The presence of proline in the protein structure destabilizes it by disrupting hydrogen bonds.
π The tertiary structure of hemoglobin is formed by the folding of the polypeptide chain, bringing distant amino acids closer.
π Hemoglobin has a quaternary structure stabilized by salt bridges and electrostatic interactions.
πββοΈ Hemoglobin can adopt two configurations: a tense, compact structure and a relaxed structure.
π¬οΈ The cooperative effect of hemoglobin allows for the facilitated binding and release of oxygen.
π©Έ Hemoglobin can transport carbon dioxide in addition to oxygen.
π§ͺ Hemoglobin has a buffering capacity that allows it to exchange oxygen for protons.
π The dissociation curve of oxygen and hemoglobin shows the difficulty and cooperativity of oxygen binding.
β‘οΈ Hemoglobin facilitates the rapid uptake of oxygen, while myoglobin is involved in oxygen storage.
π Increased production of protons and carbon dioxide leads to the Bohr effect, causing a rightward shift in the oxygen-hemoglobin dissociation curve.
π The Bohr effect results in an increased oxygen unloading capacity of hemoglobin.
β‘οΈ The release of oxygen in the blood is influenced by the accumulation of protons or carbon rings.
π΄ Increased concentrations of 23DPG and decreased levels of pH shift the oxygen dissociation curve to the right, promoting oxygen release in stored blood.
π©Έ Aging blood stored for a long time has a slower and delayed oxygen release compared to freshly donated or recently emitted blood.
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