Hemoglobin is a protein, which is composed of linked amino acids.
loss of only one amino acid from the normal hemoglobin molecule
sickle cell disease
Sickle-cell anemia
Glutamate is substituted for a valine at position 6. But this is not an amino acid problem, it's the construction of hemoglobin that's in error.
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.
A mutation in one amino acid of one of the subunits making up hemoglobin.
Sickle cell
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 A disease that involves misshaped cells that can easily cause blood clots.
prickle prums
The substitution of one triplet code in the DNA that codes for an mRNA that codes for an amino acid that makes up a protein. Sickle cell trait is an example of this. One amino acid substitution in a B chain of hemoglobin and you have an allele that will code for sickle cell trait.