The structure of the hemoglobin molecule is crucial to its function, which is to carry oxygen around the body. Hemoglobin is open like a puzzle and can absorb new oxygen, and is made up of various proteins with specific amino acid sequences. The general structure can be explained in four different ways.
Hemoglobin consists of the simplest levels of amino acids that stick together in the chain. These chains are peptides that also adhere to the heme molecule, which will eventually stick to the heme molecule. Hemoglobin differs from other proteins because the only peptide (four of them) is called a puck, not a simple protein unit.
The most common secondary protein structures are alpha IUD and beta-sheet, and each globulin contains 8 alpha IUDs. Alpha helix is the result of each globulin interacting with itself to form a stable structure.
The third structure describes how all globulins in space are bent. The heme molecule is important for the high bending hemoglobin structure, as it helps to tweak hemoglobin in shape by attaching the histidine residue too.
Of the four globulin proteins that make up hemoglobin, two are identical, called the α chain, and the other two are called the β chain, the same. It can also be called α-globin and β-globin. The quaternary composition is grouped by these units.
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