Alpha chain of haemoglobin has a 141 amino acids and it is not a protein why
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The 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. The alpha and beta chains have different sequences of amino acids, but fold up to form similar three-dimensional structures. The four chains are held together by noncovalent interactions. There are four binding sites for oxygen on the hemoglobin molecule, because each chain contains one heme group < >. In the alpha chain, the 87th residue is histidine F8 < >and in the beta chain the 92nd residue is histidine F8 >. A heme group is attached to each of the four histidines. The heme consists of an organic part and an iron atom < >. The iron atom in heme binds to the four nitrogens in the center of the protoporphyrin ring. The hemoglobin molecule is nearly spherical, with a diameter of 55 angstroms . The four chains are packed together to form a tetramer. The heme groups are located in crevices near the exterior of the molecule, one in each subunit. Each alpha chain is in contact with both beta chains.
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The 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. The alpha and beta chains have different sequences of amino acids, but fold up to form similar three-dimensional structures. The four chains are held together by noncovalent interactions. There are four binding sites for oxygen on the hemoglobin molecule, because each chain contains one heme group < >. In the alpha chain, the 87th residue is histidine F8 < >and in the beta chain the 92nd residue is histidine F8 >. A heme group is attached to each of the four histidines. The heme consists of an organic part and an iron atom < >. The iron atom in heme binds to the four nitrogens in the center of the protoporphyrin ring. The hemoglobin molecule is nearly spherical, with a diameter of 55 angstroms . The four chains are packed together to form a tetramer. The heme groups are located in crevices near the exterior of the molecule, one in each subunit. Each alpha chain is in contact with both beta chains.
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