Question

Based on what we have learned previously in this course, how do you think E3 ligase recognizes mis-folded proteins?

a. unfolded proteins are unusually bumpy
b. E3 binds to ubiquitin that got stuck inside the unfolded protein
c. E3 has hydrophobic areas that recognize that misfolded protein
d. none of the above: E2 binds to the misfolded protein, not E3

Answer 1

E3 ligase recognizes mis-folded proteins by using its hydrophobic areas to bind to exposed hydrophobic regions on the misfolded protein.

Step-by-step explanation:

E3 ligase recognizes mis-folded proteins through a process involving the hydrophobic areas of the E3 ligase. When a protein is misfolded, it exposes hydrophobic regions that are normally buried in the correctly folded protein. The hydrophobic areas of the E3 ligase can recognize and bind to these exposed hydrophobic regions of the misfolded protein, marking it for degradation.