#Question id: 863
#Unit 1. Structure and Function of Biomolecules
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: 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).