Final answer:
Deletion of an amino acid (AA) on the CFTR protein due to a frameshift mutation can dramatically affect its structure, resulting in a nonfunctional protein or termination of protein synthesis. In cystic fibrosis, this deletion leads to the production of a defective CFTR protein that cannot properly transport chloride ions out of the cell, causing the development of CF symptoms.
Step-by-step explanation:
Deletion of an amino acid (AA) on the cystic fibrosis transmembrane conductance regulator (CFTR) protein can have a dramatic impact on its structure because it can lead to a frameshift mutation. A frameshift mutation occurs when one or more nucleotides are inserted or deleted, causing a shift in the reading frame of the mRNA. As a result, the entire protein message is changed, creating a nonfunctional protein or terminating protein synthesis altogether. For example, in the case of CF, the deletion of an AA on CFTR due to a frameshift mutation can result in the production of a defective CFTR protein that is not properly incorporated into the cell membrane. This defective protein cannot effectively transport chloride ions out of the cell, which is the normal function of CFTR in healthy individuals. The ultimate result is a malfunctioning ion channel and the development of symptoms associated with cystic fibrosis.