Question

4. Based on the structure of individual keratin subunits, why would a single point mutation in the alpha-helical region of the monomer result in a defect in the polymer? Be sure to explain it from the standpoint of DNA and intermediate filament structure.

Answer 1

According to the given question, the description follows as the points change in keratin is a case of cytoskeleton issue. α-keratin is a stringy basic protein, made up of amino acids that structure a rehashing auxiliary structure and this optional structure frames a snaked curl. Through disulfide bonds, they structure a protofilament and the two protofilaments total to frame a protofibril, and four protofibrils polymerize to shape the transitional fiber and this fiber is the fundamental subunit of α-keratins Keratin fills in as auxiliary and defensive capacities, especially in the epithelium.

The point transformation is a hereditary transformation, where a solitary nucleotide base in DNA arrangement is changed and this transformation in DNA modifies the mRNA and consequently adjusts the amino corrosive chain. Thus, the wrong amino corrosive getting created, which changes the protein, and this reason issues the polymeric protein structure.

The single point transformation in polypeptide chains influences the winding and in this manner impacts the development of left-gave helical structure known as a looped curl. The point transformation in α-keratin in this way influences its capacities.