Sickle cell anemia is caused by a mutation in a single amino acid in the hemoglobin chain. A glutamate is mutated to valine. What would be the effect of such a change?

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Casey DurganLv2

2 Jul 2018

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Related questions

Below is the protein sequence for the beta subunit of human hemoglobin (using the one letter abbreviations for amino acids). Use it to answer the following questions.

Write the order of the LAST 10 amino acids in this protein.

For each of the LAST 10 amino acids, tell one other amino acid that it would favorably interact with (i.e. could form a bond with).

In sickle cell anemia, the first glutamate (E) is mutated to valine (V). Propose a hypothesis on how this change of amino acid will affect the folding of the hemoglobin protein and why the hemoglobin function will change.

 MVHLTPEEKSAVTALWGKVNVDEVGGEALGRLLVVYPWTQRFFESFGDLSTPDAVMGNPKVKAHGKKVLGAFSDGLAHLDNLKGTFATLSELHCDKLHVDPENFRLLGNVLVCVLAHHFGKEFTPPVQAAYQKVVAGVANALAHKYH

Insickle cell anemia, the first glutamate (E) is mutated to valine(V). Propose a hypothesis on how this will affect the folding ofthe hemoglobin.

In most cases of sickle-cell anemia, where the 6th amino acid (typically glutamate) is replaced by valine, how would the potential for chemical interactions change? (You may need to look up the structures in your textbook or online).

A. Valine will form fewer covalent bonds in the protein backbone.

B. Valine will form fewer ionic bonds with other side-chains

C. Valine will form fewer hydrophobic interactions with other side-chains

D. Nothing will change because valine and glutamate have very similar chemical properties