How does GT recognize incompletely folded or misfolded proteins that have been recently synthesized?
A)Such proteins display exposed hydrophilic residues that are absent from properly folded proteins.
B)Five histidine residues are exposed on the protein's surface when it is improperly folded.
C)Such proteins display exposed hydrophobic residues that are absent from properly folded proteins.
D)Six arginine residues are exposed on the protein's surface when it is improperly folded.
E)Such proteins display numerous carboxyl groups on their surfaces,which decreases their solubility.

Question

Quizplus · Accepted Answer

Incompletely folded or misfolded proteins are recognized by GT based on the exposure of hydrophobic residues on their surfaces, which are normally buried in the interior of properly folded proteins. This is because GT contains chaperones such as Hsp70 and Hsp90 that have hydrophobic binding sites that can interact with the exposed hydrophobic patches on the misfolded proteins, leading to their refolding or degradation. Exposed hydrophilic residues (choice A) and carboxyl groups (choice E) are not specific features of misfolded proteins and do not play a significant role in their recognition by GT. Likewise, the exposure of five histidine residues (choice B) or six arginine residues (choice D) on the protein's surface is not a well-established mechanism for GT recognition of misfolded proteins.

How Does GT Recognize Incompletely Folded or Misfolded Proteins That