yes
The type of mutation that causes a defect in the gene (causing sickle cell anaemia) is a substitution mutation.A single nucleotide substitution (A to T) in the β-globin gene causes the amino acid valine to replace glutamic acid. This changes the resulting protein, causing a haemoglobin with an abnormal shape to be created.
Substitution of Val for Glu in the 6th amino acid may disrupt protein structure and function, as these amino acids have different properties. Valine is hydrophobic and bulky, while glutamic acid is hydrophilic and negatively charged. This change could impact protein folding, stability, and interactions with other molecules.
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.
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.
The disease sickle cell anaemia occurs due to a mutation. This causes the amino acid glutamic acid (which is hydrophilic) in haemoglobin to be replaced by valine (which is hydrophobic).
A single amino acid substitution, such as the one in sickle cell anemia where glutamic acid is replaced by valine, can cause hemoglobin molecules to stick together due to a change in the structure of the protein. This structural change leads to the formation of abnormal hemoglobin polymers that can distort the shape of red blood cells, leading to their sickling and contributing to various complications.
The gene associated with sickle cell anemia is HBB, which is located in region 15.5 on the short arm of chromosome 11. There are many variations that can cause sickle cell, but primarily it is caused by the hemoglobin variant Hb S. According to the human genome project website: "the hydrophobic amino acid valine takes the place of hydrophilic glutamic acid at the sixth amino acid position of the HBB polypeptide chain. This substitution creates a hydrophobic spot on the outside of the protein structure that sticks to the hydrophobic region of an adjacent hemoglobin molecule's beta chain. This clumping together (polymerization) of Hb S molecules into rigid fibers causes the "sickling" of red blood cells." In a nutshell, when the hydrophobic (water fearing) amino replaces a hydrophilic one (water loving) on the protein chain, it creates a spot that sticks to another similar mutated gene, and they clump together, creating a sickle shaped cell. Looking at the location and incidence rates of sickle cell amenia, scientists believe that because malaria rates are high in the region, the body has created this defense against the disease -- an evolutionary self defense. Hope that helps :-)
Valine is an amino acid, one of the biochemical components of proteins. A protein can consist of hundreds of amino acids. So valine is not a protein but a part of a protein in the way that one piece is not an entire jigsaw puzzle :).
Sickle cell anaemia is such a genetic disease. The sixth amino acid in the beta chain of haeme which is glutamic acid in normal people gets replaced by valine in sickle cell anaemia patients. This simple change in the amino acid sequence results in the the sickle shape of RBCs
Normally, the 6th position of the beta chain of hemoglobin is a Glutamic acid, encoded on the DNA as GAG. The sickle cell mutation has the sequence GTG, resulting in a Valine in the 6th position instead.
valine
If a single amino acid is changed in a protein sequence, it can lead to a change in the protein's structure and function. This change can result in a loss of function, altered function, or gain of function, depending on the specific amino acid substitution and its location within the protein. Denaturation or misfolding of the protein may also occur in some cases.