#Question id: 857
#Part-B Specialized Branches in Biotechnology
The aggregation of nonpolar side chains in the interior of a protein is favored by
#Question id: 859
#Part-B Specialized Branches in Biotechnology
Which one statement is incorrect about ATG genes;
#Question id: 861
#Part-B Specialized Branches in Biotechnology
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: 863
#Part-B Specialized Branches in Biotechnology
Ubiquitinated proteins are proteolytically degraded in an ATP-dependent process mediated by a large (∼2500 kD, 26S) multiprotein complex named the 26S proteasome;
#Question id: 865
#Part-B Specialized Branches in Biotechnology
In autophagy, the endoplasmic reticulum (ER) first gives rise to a cup-shaped, membranous cisterna called the______
#Question id: 869
#Part-B Specialized Branches in Biotechnology
Which statements are correct regarding protein folding
A. Many molecular chaperones were first described as heat shock proteins (Hsp) because Their rate of synthesis is increased at elevated temperatures
B. The renaturation of a denatured protein in vitro may not entirely mimic the folding of a protein in vivo.
C. Molecular chaperones are essential proteins that bind to only partially folded polypeptide chains.
D. Molecular chaperones function to lift folding polypeptides out of the false minima in their folding funnel.