#Question id: 864
#Unit 1. Structure and Function of Biomolecules
Which one is not the appropriate function of Heat Shock Proteins;
#Question id: 865
#Unit 1. Structure and Function of Biomolecules
In autophagy, the endoplasmic reticulum (ER) first gives rise to a cup-shaped, membranous cisterna called the______
#Question id: 866
#Unit 1. Structure and Function of Biomolecules
Which of the following is known as Sanger’s reagent
#Question id: 867
#Unit 1. Structure and Function of Biomolecules
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. Structure and Function of Biomolecules
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. Structure and Function of Biomolecules
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.