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
(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
Ans: (A) properties of the molecule as a result of abnormal interactions between adjacent hemoglobin molecules
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