Answer:
The answer is D) It will affect the primary, secondary, and tertiary structures of the CFTR protein.
Explanation:
The deletion of phenylalanine (F) in position 508 or F508, <u>disrupts the sequence of amino acids and polypeptides</u>, as seen in the <u>primary structure</u>.
It also affects the <u>secondary structure</u> since it can <u>alter the folding or kinks of the alpha-helices or beta-sheets</u> of the local polypeptide chain.
For the <u>tertiary structures</u>, it will <u>affect the overall shape of the CFTR protein</u>, and ultimately, <u>alter its function in the body</u> which is to produce thin, free-flowing mucus in the respiratory, digestive, and reproductive system, etc.
<h3>What is the CFTR Protein?</h3>
Normally, the Cystic Fibrosis Transmembrane Conductance Regulator (CFTR) protein functions as a <u>membrane channel protein</u> that transports negatively-charged ions, such as <u>chloride ions</u>, in and out of the cell. It also <u>transports water</u> which is used to <u>form thin, free-flowing mucus</u> seen in the <u>respiratory, digestive, and reproductive systems</u>. It can also influence other channels to <u>regulate the entry of sodium ions across plasma membranes</u> seen in the <u>pancreas and lungs</u>.
The CFTR protein mutation found in Cystic Fibrosis (CF) is present in almost <u>70% of CF patients</u>. The mutation <u>alters the structure of the chloride ion channel</u> and movement of chloride ions and water in and out of the cell. Thus, <u>impairing the production of mucus, which is characteristically sticky and thick</u> seen in Cystic Fibrosis.
