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Sickle-cell anemia results from a point mutation in the HBB gene. The mutation results in the replacement of an amino acid that has a hydrophilic R-group with an amino acid that has a hydrophobic R-group on the exterior of the hemoglobin protein. Such a mutation would most likely result in altered

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Answer: protein structure

Explanation:

In Sickle-cell anemia, the gene sequence of hemoglobin is changed in its sixth position due to the substitution of glutamate with valine.

So, since glutamate, an amino acid soluble in water due to its hydrophilic side chain is substituted with valine, an amino acid that has a hydrophobic side chain insoluble in water or bloodstream; the resulting hemoglobin protein is altered in structure (sickle shaped) and unable to bind and transport oxygen efficiently to the various body parts.

Answer:

A. properties of the molecule as a result of abnormal interactions between adjacent hemoglobin molecules

Explanation:

This question is from the 2012 AP Biology Practice Exam. The choices are:

  • A. properties of the molecule as a result of abnormal interactions between adjacent hemoglobin molecules
  • B.  DNA structure as a result of abnormal hydrogen bonding between nitrogenous bases
  • C. fatty acid structure as a result of changes in ionic interactions between adjacent fatty acid chains
  • D. protein secondary structure as a result of abnormal hydrophobic interactions between R-groups in the backbone of the protein

See the attached two images for the answer choices and why choice A is correct!

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