NEET BIOLOGY

Detailed explanation-1: -Hemoglobin, in the normal adult, is a protein whose main function is to transport oxygen from the lungs to tissues and to transport carbon dioxide from tissues to the lung. The hemoglobin molecule contains four separate folded peptide chains, which form a hydrophobic or water ‘repelling’ pocket around a heme group.

Detailed explanation-2: -Hemoglobin contains iron, which allows it to pick up oxygen from the air we breathe and deliver it everywhere in the body. You can think of hemoglobin as the iron ("heme"), oxygen transport protein, ("globin") found in red blood cells. It’s the hemoglobin that gives red blood cells their color, too.

Detailed explanation-3: -Like all proteins, it is made up of small molecules called amino acids. A hemoglobin molecule is made up of four polypeptide chains, two alpha chains of 141 amino acid residues each and two beta chains of 146 amino acid residues each.

Detailed explanation-4: -Hemoglobin is a protein found in red blood cells (RBCs) that is comprised of two alpha and two beta subunits that surround an iron-containing heme group. Oxygen readily binds this heme group. The ability of oxygen to bind increases as more oxygen molecules are bound to heme.

Detailed explanation-5: -In the hemoglobin, there are three key amino acid residues responsible for the bind of oxygen to the active site: lysine (Lys), histidine (His), and aspartate (Asp). The three amino acids are linked by two salt bridges.