#Question id: 865
#Unit 1. Molecules and their Interaction Relevant to Biology
In autophagy, the endoplasmic reticulum (ER) first gives rise to a cup-shaped, membranous cisterna called the______
#Question id: 866
#Unit 1. Molecules and their Interaction Relevant to Biology
Which of the following is known as Sanger’s reagent
#Question id: 867
#Unit 1. Molecules and their Interaction Relevant to Biology
Match the correct diseases with their precursors
|
Disease |
Protein or precursor involved in disease |
|
1. Cystic fibrosis |
a. Prion protein |
|
2. Creutzfeldt–Jakob disease |
b. CFTR |
|
3. Familial hypercholesterolaemia |
c. LDL receptor |
|
4. fatal familial insomnia |
d. β-amyloid protein |
|
5. Alzheimer’s disease |
e. β-hexosaminidase |
#Question id: 868
#Unit 1. Molecules and their Interaction Relevant to Biology
Which statements is incorrect about ‘The chaperonin-assisted catalysis of protein folding’
A. The non-cooperative nature of ATP binding establishes GroEL as an allosteric enzyme.
B. In GroEL with a total of 14 subunits in two heptameric rings are observed.
C. In vivo GroES is composed of seven identical subunits whilst GroEL is composed of 14 larger subunits.
D. Gro-EL being called chaperonin60 (cpn60) and Gro-ES chaperonin10 (cpn10).
#Question id: 869
#Unit 1. Molecules and their Interaction Relevant to Biology
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: 870
#Unit 1. Molecules and their Interaction Relevant to Biology
Choose correct statements about ‘Protein Disulfide Isomerase’ in protein folding
A. Oxidized PDI catalyzes the rearrangement of a polypeptide’s non-native disulfide bonds via disulfide interchange reactions to yield native disulfide bonds.
B. Reduced PDI catalyzes the initial formation of a polypeptide’s disulfide bonds through the formation of a mixed disulfide.
C. Protein disulfide isomerase contains the conserved active site motif of Cys-Xaa-Xaa-Cys found in thioredoxin and shares a similar role to the Dsb family of proteins found in E. coli.
D. Under more reducing conditions with thiols in the active site the enzyme reshuffles disulfides (isomerase) in target proteins.