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Hemoglobin is a tetramer consisting of two α-chains and two β-chains.
Both hemoglobins are tetramers, each consisting of two α-chains and two β-chains.
In this complex, protein is heterodimeric in nature, consisting of two α-chains (451 residues), two β-chains (452 residues) and the Stathmin-like domain (142 residues).
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Haptoglobin is a polypeptide structurally consisting of two α chains (α1 or α2) and two β chains.
Their main constituent is Collagen IV, a helical trimer consisting of three α chains, capable of forming polymeric networks that interact with other ECM proteins.
Collagen IX is a hetero-trimeric molecule that consists of three α chains, α1(IX), α2(IX), and α3(IX)) in a 1 1 1 ratio.
Haptoglobin is a complex tetramer glycoprotein, consisting of two α and two β chains, synthesised mainly by the liver [ 80].
Human hemoglobin in adults is for the most part hemoglobin A, a four-component molecule consisting of two α and two β hemoglobin chains.
Adult hemoglobin (HbA) exists as a tetramer of noncovalently bound globin chains, consisting of two α and two β subunits.
Normal hemoglobin (HbA) consists of two α- and two β-globin chains.
It consists of two α-helical domains classified as mainly alpha orthogonal bundles by CATH.
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