BICH 410 Lecture Notes - Lecture 13: Protein Quaternary Structure, Alpha Helix, Myoglobin
Document Summary
Myoglobin (in muscles) & hemoglobin (in blood) are important oxygen binding proteins Help illustrate reverse binding of a ligand to a protein. As o2 is brought into the body co2 is needed to be pushed out of the body co2 is considered waste that isn"t detrimental to the breathing process. The heterotetramer structure of hemeglobin is allowed to carry 4 molecules of oxygen. Hemoglobin picks up the o2 transfers to myoglobin and then drops it off around the body where it is needed. Both myoglobin and hemoglobin are both heavy in alpha helix structures. Heme means? contains a prosethetic group which is a protoporphyrin ring with an iron ion. Each subunit is myoglobin like containing 8 alpha helical segments with different turning connecting segments. Even though it has two different descriptions all subunits are all motifs of alpha helices. High degree of hydrophobic pockets with heme groups within.
