Beta-Globin
6th amino acid is changed in haemoglobin chain due to a recessive mutation on beta haemoglobin producing gene
Hemoglobin S. This the predominant hemoglobin in people with sickle cell disease. The alpha chain is normal. The disease-producing mutation exists in the beta chain, giving the molecule the structure, a2bS2. People who have one sickle mutant gene and one normal beta gene have sickle cell trait which is benign.
A beta-folded sheet is a secondary structure of a protein, which is the next level of molecular organization above the primary structure. It is formed by hydrogen bonding between adjacent segments of a polypeptide chain, creating a flat and elongated sheet-like structure.
Hemoglobin is the main constituent of red blood cells, and as such, it belongs to the circulatory system.
glutamic acid is replaced by valine in the beta chain
Fetal hemoglobin has a pair of gamma-globin molecules in place of the typical beta-globins of adult hemoglobin
Hemoglobin produced in association with the sickle cell trait; the beta-globin molecules of hemoglobin S are defective.
Beta particles are not stopped by a paper sheet.
4 months
Normal adult hemoglobin has a pair each of alpha-globin and beta-globin molecules
Beta-Globin
Thin sheet or plastic may prevent beta particles.
There are four nearly-identical individual protein chains in hemoglobin.
The minimum protection against exposure to beta particles is a thin sheet of metal or plastic. Beta particles are classified as subatomic particles.
6th amino acid is changed in haemoglobin chain due to a recessive mutation on beta haemoglobin producing gene
2 Alpha Globins and 2 Beta Globins