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Multiple Choice
Patients with sickle-cell anemia disease have a point mutation leading to a single amino acid substitution in the hemoglobin protein, causing it to alter its shape/function. Which amino acid substitution most likely causes the disease?
A
Ser to Thr
B
Arg to Lys
C
Val to Leu
D
Glu to Val
Verified step by step guidance
1
Understand the context: Sickle-cell anemia is caused by a mutation in the hemoglobin protein, specifically in the beta-globin chain.
Identify the mutation: The disease is caused by a point mutation where the amino acid glutamic acid (Glu) is replaced by valine (Val) at the sixth position of the beta-globin chain.
Consider the properties of the amino acids: Glutamic acid is a polar, negatively charged amino acid, while valine is a nonpolar, hydrophobic amino acid. This change affects the solubility and structure of hemoglobin.
Analyze the impact of the substitution: The substitution of Glu to Val leads to the formation of hemoglobin S (HbS), which causes the hemoglobin molecules to stick together, forming fibers that distort red blood cells into a sickle shape.
Conclude the effect: The sickle-shaped cells can block blood flow in small vessels, leading to the symptoms of sickle-cell anemia, such as pain and organ damage.