#Question id: 855
#Unit 1. Molecules and their Interaction Relevant to Biology
Which of the following interactions make a large contribution to the stability of protein structures
#Question id: 856
#Unit 1. Molecules and their Interaction Relevant to Biology
Protein folding is not a completely random, trial-and-error process, This problem was first pointed out by
#Question id: 857
#Unit 1. Molecules and their Interaction Relevant to Biology
The aggregation of nonpolar side chains in the interior of a protein is favored by
#Question id: 858
#Unit 1. Molecules and their Interaction Relevant to Biology
Unfolded protein response (UPR)
#Question id: 859
#Unit 1. Molecules and their Interaction Relevant to Biology
Which one statement is incorrect about ATG genes;
#Question id: 860
#Unit 1. Molecules and their Interaction Relevant to Biology
Select true âTâ AND false âFâ 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.