How does UGGT 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 display exposed hydrophobic residues on their surfaces that are absent from properly folded proteins. UGGT recognizes these exposed hydrophobic residues and adds a glucose molecule to the N-linked glycan, marking the protein for further chaperone-assisted folding or degradation.

How Does UGGT Recognize Incompletely Folded or Misfolded Proteins That