Molecular chaperones are different from chaperonins

Info iconThis preview shows page 1. Sign up to view the full content.

View Full Document Right Arrow Icon
This is the end of the preview. Sign up to access the rest of the document.

Unformatted text preview: PrPSc are protein forms associated with prion ­based disorders. They share the same: a. Post ­translational modification b. Tertiary structure c. Stability d. Amino acid sequence e. Susceptibility to denaturation 16. A leading cause of protein misfolding is inappropriate non ­covalent interactions, specifically inappropriate: a. Hydrophobic interactions b. Van der Waals interactions c. Hydrogen bonds d. Ionic bonds e. Disulfide bonds 17. Molecular chaperones are different from chaperonins. This is because molecular chaperones are: a. ATP dependent b. Help proteins fold correctly c. Create a hydrophilic environment to ‘force’ misfolded proteins to fold correctly d. Bind and stabilize hydrophobic regions of a nascent polypeptide e. Directly facilitate the folding of proteins 18. When ATP binds to the chaperonin GroEL, the chamber relaxes. What happens next? a. The GroES cap can bind b. The misfold...
View Full Document

{[ snackBarMessage ]}

Ask a homework question - tutors are online