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Hemoglobin consists of protein subunits (globin molecules), which are polypeptides, long folded chains of specific amino acids which determine the protein's chemical properties and function. The amino acid sequence of any polypeptide is translated from a segment of DNA, the corresponding gene. There is more than one hemoglobin gene.
Two globin chains that have heme groups combine to form hemoglobin. One of the chains is an alpha chain and the other is a non-alpha chain. Non-alpha chain nature in hemoglobin molecules varies due to different variables. Fetuses have a non-alpha chain called gamma and after birth it is then called beta. The beta chain will pair with the alpha ...
n/a Ensembl ENSG00000223609 n/a UniProt P02042 n/a RefSeq (mRNA) NM_000519 n/a RefSeq (protein) NP_000510 n/a Location (UCSC) Chr 11: 5.23 – 5.24 Mb n/a PubMed search n/a Wikidata View/Edit Human Hemoglobin subunit delta is a protein that in humans is encoded by the HBD gene. Function The delta (HBD) and beta (HBB) genes are normally expressed in the adult: two alpha chains plus two beta ...
Hemoglobin variants occur when there are mutations in specific genes that code for the protein chains, known as globins, which make up the hemoglobin molecule. This leads to amino acid substitutions in the hemoglobin molecule that could affect the structure, properties, and/or the stability of the hemoglobin molecule.
These have one, two, four, or eight iron atoms that are each approximately tetrahedrally coordinated to four sulfur atoms; because of this tetrahedral coordination, ths in the surrounding peptide chains. Another important class of iron–sulfur proteins is the ferredoxins, which have multiple iron atoms. Transferrin does not belong to either of ...
In human, the HBB gene is located on chromosome 11 at position p15.5.. Hemoglobin subunit beta (beta globin, β-globin, haemoglobin beta, hemoglobin beta) is a globin protein, coded for by the HBB gene, which along with alpha globin (), makes up the most common form of haemoglobin in adult humans, hemoglobin A (HbA). [5]
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The most famous mutation in the globin fold is a change from glutamate to valine in one chain of the hemoglobin molecule. This mutation creates a "hydrophobic patch" on the protein surface that promotes intermolecular aggregation, the molecular event that gives rise to sickle-cell disease. [citation needed]