Exam 31: Completing the Protein Life Cycle: Folding, Processing, and Degradation

In general, proteins whose folding is chaperone-dependent start the folding process first with ____ and then are passed as ____ folded intermediates to ____.

Proteins with ____ sequences remain embedded in the ER membrane with their ____-termini on the cytosolic face of the ER.

The primary driving force for folding is/are ____ and if crowding occurs then ____ is likely.

Mitochondrial presequences are ____ charged amphipathic sequences retained in the ____ stage through association with ____ molecular chaperones.

Characteristics of protein translocation systems include all EXCEPT:

A highly conserved protein that is involved in protein degradation is:

All are characteristics of HtrA proteases EXCEPT:

Protein degradation is compartmentalized either in macromolecular structures known as ____ or in degradative organelles such as ____.

The most common form of post-translational processing is:

The proper sequence for transport of mitochondrial matrix proteins would be:

Characteristics of Hsp90 chaperones include all EXCEPT:

Which of the following statements regarding chaperones and chaperonins is correct?

____ recognize the sorting signals as they emerge from the ribosome and together with ____ deliver the nascent protein chain to specific membrane complexes called ____ that mediate integration into and across the membrane.

The folding cycle in the GroES-GroEL complex of E. coli utilizes the following sequence: A.ATP binding to GroEL B.GroES dissociates from the complex C.Partially folded protein hydrophobic residues bind GroEL D.GroES is recruited to GroEL E.GroES promotes ATP hydrolysis and α-subunits undergo a conformational change that buries the hydrophobic patches

Which of the following is a result of the sumoylation of a protein?

Which of the following statements about protein folding is INCORRECT?