29. In sickle cell anemia, a hereditary disease, there is substitution of one amino acid by another in one of the four polypeptide chains of hemoglobin. In this case are all of the structural levels of the protein modified?

Describe the effect of the amino acid change on protein function: how does the HbS protein function differently than the HbA protein in red blood cells?

Sickle cell anemia is a horrific molecular disease that causes a multitude of issues within the human body, despite the disease’s hemoglobin only slightly varying in structure, as normal hemoglobin’s glutamic acid is instead replaced with valine in the beta-globin amino acid chain. By only changing structurally in this slight amount , sickle cell takes on its unique shape which then causes a multitude of issues within the human body. How does the replacement of glutamic acid with valine end up resulting in this shape, and how would it affect its interaction with the rest of the body?

In what type of intra and intermolecular interactions does a valine within a protein backbone typically participate? How would this variation in Sickle Cell Disease be classified?