malaria
Sickle cell hemoglobin differs from normal hemoglobin primarily due to a single amino acid substitution in the hemoglobin protein chain. In sickle cell disease, a person inherits two copies of an abnormal hemoglobin gene, usually referred to as HbS. In normal hemoglobin (HbA), the amino acid glutamic acid is present at a specific position in the beta chain of the hemoglobin protein. However, in sickle cell hemoglobin (HbS), this glutamic acid is replaced by valine due to a genetic mutation. This change causes the hemoglobin molecules to stick together under certain conditions, forming long, rigid structures that distort red blood cells into a sickle or crescent shape.
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.
The amino acid sequence of the sickle cell allele for hemoglobin varies from the normal allele for hemoglobin by one amino acid. The sickle cell allele for hemoglobin has valine instead of glutamic acid. When the oxygen level of the blood decreases, the hemoglobin molecules come out of solution, stick together, and form long chains that cause the red blood cells to become sickle shaped.
Sickle cell disease is caused when someone inherits sickle shaped hemoglobin. It is a disease that can be managed, but not cured.
The pro of sickle cell hemoglobin is that if you have only one allele for sickle cell hemoglobin and the other allele is normal, then you are immune to malaria.
malaria
Hemoglobin
It is Hemoglobin
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Matt Jones has herpes in the butt hole!
because of the change of AA- in normal cell- from Glutamic acid (negativity charged) to Valine (uncharged) -in sickle cell- the charge will be missing in the sickle cell that why the electrophoresis will become slower because of the missing charge
Sickle cell disease is a mutation in the gene that codes for hemoglobin, which causes the hemoglobin and the cell to become elongated and look like a sickle rather than its normal disc shape.
because of the change of AA- in normal cell- from Glutamic acid (negativity charged) to Valine (uncharged) -in sickle cell- the charge will be missing in the sickle cell that why the electrophoresis will become slower because of the missing charge
Sickle cell hemoglobin differs from normal hemoglobin primarily due to a single amino acid substitution in the hemoglobin protein chain. In sickle cell disease, a person inherits two copies of an abnormal hemoglobin gene, usually referred to as HbS. In normal hemoglobin (HbA), the amino acid glutamic acid is present at a specific position in the beta chain of the hemoglobin protein. However, in sickle cell hemoglobin (HbS), this glutamic acid is replaced by valine due to a genetic mutation. This change causes the hemoglobin molecules to stick together under certain conditions, forming long, rigid structures that distort red blood cells into a sickle or crescent shape.
Sickle-cell anemia
loss of only one amino acid from the normal hemoglobin molecule