#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.
#Question id: 872
#Part-B Specialized Branches in Biotechnology
Which of the following statements is not true about HSP 70 family.
A. They have a molecular weight near 70,000 and are abundant in cells stressed by elevated temperature.
B. Bind to regions of unfolded polypeptides that are rich in hydrophilic residues
C. Hsp70 proteins not block the folding of certain proteins that must remain unfolded untill they have been translocated across a membrane.
D.) It releases polypeptides in a cycle that uses energy from ATP hydrolysis.
#Question id: 875
#Part-B Specialized Branches in Biotechnology
Why positive phi angles less common than negative Phi angles in proteins contain L amino acid?