You are screen sharing Stop Share Question 6 5 pts Assume a new protein named Wigglin, which contains over 1000 amino acids, has been discovered by OSU researchers. One of the members of the discovery team, a student from BB 450, has noticed that the shape of Wigglin (its folded 3D structure) is drastically changed when it is dropped from neutral pH (where it has roughly a spherical shape) into the acidic environment of the digestive juice of a carnivorous pitcher plant (where Wigglin now gains an overall shape sort of like a starfish). What is additionally remarkable about the observation is that in comparing the two shapes of Wigglin, some of the bonds of the polypeptide backbone that are expected to be able to rotate have indeed shown substantial bond rotation, but the majority of bonds that are typically free to rotate do not vary by even a single degree of rotation when Wigglin takes its plunge into the pitcher plant. What is the most plausible explanation for the lack of bond rotation among the following choices? Hydrogen bonding explains all. The change in pH created cross links that hold most rotatable bonds in place Though the single bonds of the polypeptide backbone can rotate, clashes between chemical groups such as side chains may hinder or prevent rotations. The polypeptide backbone includes a peptide bond in every third position, explaining the lack of rotation that was observed. O Proteins that are large (e.g. 1000 amino acids) are too massive to allow free bond rotations. 20 DOE DOS FS 59 FB FO 2 uc ar # 3 $ 4 Serent shot for selected ara % 5 & 7 TOWER 6 8 9 w E R. T Y