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.
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
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.
sickle cell anemia
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).
sickle cell anemia
sometime nothing- If the substituted amino acid (AA) is chemically similar (in terms of polarity, acid/base, size) to the original, the protein might be able to function without problem. However, if the substitution is to a very different AA, then drastic changes can occur. If the wrong AA is sequenced, then the protein might misfold (improper tertiary structure, tertiary structure is determined by primary structure- sequence of AA). If you get a misfolded protein, it might not function as well or at all. Note that Sickle Cell Disease is caused by a Valine-Glutamine substitution. This results is a misfolded hemoglobin that causes the RBCs to "sickle". Thus, this reduces their oxygen carrying capacity.
yes. thymine replaces adenine in the dna that codes for the amino acid on the 6th position of the beta globin chain resulting in an amino acid change of glutamic acid to valine. shari (med student - jamaica)
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 :).
amino acids
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.