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28 Nov 2019

Which of the following is NOT true?

A)

Protein re-folding may be ATP-driven through chaperones.
B)

Polyubiquitylation of a protein targets a protein to the lysosome for destruction.
C)

Unfolded or misfolded proteins may be either re-folded or destroyed.
D)

Protein re-folding may be spontaneous.

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Related questions

Some proteins, once folded “associate” to form higher order structures (i.e., quaternary structure). Within these structures the single protein chain is known as a “subunit” (not to be confused with a protein domain). If two identical protein chains fold and associate, the quaternary structure is named “homodimer” (and the individual subunits are sometimes referred to as “monomers”); for three “homotrimer” and so on. If, on the other hand, the two protein chains that associate have different primary structures, the quaternary structure is named “heterodimer”. Using the dimer as an example, we know that the respective regions of the protein subunit surfaces that are interfaced, are responsible for the “favorable energy of interaction” which stabilizes the dimeric protein complex.

(a). Although, noncovalent bonding interactions are used both for stabilization of the folded protein molecule and its dimerization, the contribution of the “hydrophobic effect” to chain folding is significantly greater than its contribution to subunit association. Define the “hydrophobic effect” and explain why you would expect it to have a more pronounced role in chain folding compared to dimerization of the folded molecules.

(b) As the protein chain folds to the native structure, it loses entropy. Upon dimerization, more protein entropy is lost. Compare and contrast the source of protein entropy loss, which occurs with folding, with that which occurs with dimerization.

Which of the following statements about proteins conformations is/are true? Select all that apply.

A. A stable folded conformation of a protein has the maximum number of favorable non covalent interactions.

B. Unfolded proteins are unstable.

C. A native conformation of a protein is the functional conformation.

D. Hydrophobic interactions (i.e. the hydrophobic effect) make the greatest contribution to protein stability.

E. All proteins have only a single stable conformation.

Which of the following is triggered by the accumulation of misfolded proteins in the ER? A Option A: inhibition of the trans Golgi network B Option B: activation of the cis Golgi network C Option C: reduced transcription of rRNA D Option D: the unfolded protein response

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