Describe how a single amino acid substitution causes hemoglobin molecules to stick together. Use what you know about the structure of hb and hbs

Question: Describe how a single amino acid substitution causes hemoglobin molecules to stick together. Use what you know about the structure of Hb and HbS, the properties of glutamic acid and valine, and how hydrophobicity causes molecules to behave in water.

Answer:

A Single amino acid must be polar to attract, just like water.

Explanation:

Sickle cell is an genetic illness and it is began by a alteration that arises in the beta sub units of the haemoglobin. Haemoglobin is a tetrameric protein made up of 2 alpha sub units and 2 beta sub units and it is the important part of the blood accountable for oxygen passage. Sickle cell is a illness that consequences from a replacement of a polar amino acid identified as glutamate with a non polar one valine at site six of the beta polypeptide component of haemoglobin. The replacement occurs as a consequence of a alteration in one of the bases in the beta-globin gene from adenine to thymine. As a outcome of this change, the beta polypeptide chains convert sticky in low oxygen circumstances since the valine sticks out of the chain and interrelates with neighboring non-polar amino acids.