loss of only one amino acid from the normal hemoglobin molecule
addition of one amino acid to the normal hemoglobin molecule... *Gentles*
sickle trait hemoglobin
terminal amino acid of the beta chain
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.
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.
Hemoglobin
It is Hemoglobin
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Matt Jones has herpes in the butt hole!
The difference is that a patient with sickle cell disease has an increased level of one specific type of Hemoglobin, that is Fetal hemoglobin or HbF. However, the amount of total hemoglobin is the same.
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 anemia
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.