#Question id: 858
#Unit 1. Structure and Function of Biomolecules
Unfolded protein response (UPR)
#Question id: 859
#Unit 1. Structure and Function of Biomolecules
Which one statement is incorrect about ATG genes;
#Question id: 860
#Unit 1. Structure and Function of Biomolecules
Select true ‘T’ AND false ‘F’ about ubiquitinylation
I. These ubiquitin-like modifiers control processes as diverse as nuclear import,
II. Regulated by the ubiquitin-like modifier Sumo, and autophagy,
III. Regulated by the ubiquitin-like modifier Atg8.
IV. For a protein to be efficiently degraded, it must be linked to a chain of at least four tandemly linked ubiquitin molecules in which Lys 34 of each ubiquitin forms an isopeptide bond with the C-terminal carboxyl group of the following ubiquitin.
#Question id: 861
#Unit 1. Structure and Function of Biomolecules
Alexander Varshavsky discovered, the half-lives of many cytoplasmic proteins vary with the identities of their N-terminal residues via the so-called N-end rule:-
|
A. Destabilizing N-terminal residues Asp, Arg, Leu, Lys, and Phe have half-lives of |
i. Only 2 to 3 minutes, |
|
B. Stabilizing N-terminal residues Ala, Gly, Met, Ser, Thr, and Val have half-lives of |
ii. >10 hours in prokaryotes iii. >20 hours in eukaryotes. |
#Question id: 862
#Unit 1. Structure and Function of Biomolecules
Match the following
| lysosomal protein degradation pathways | Found in | |
| 1. Nonselective | a-well-nourished cells | i-containing the pentapeptide Lys-Phe-Glu-Arg-Gln |
| 2- Selective | b-starving cells |
#Question id: 863
#Unit 1. Structure and Function of Biomolecules
Ubiquitinated proteins are proteolytically degraded in an ATP-dependent process mediated by a large (∼2500 kD, 26S) multiprotein complex named the 26S proteasome;