#Question id: 910
#Unit 1. Structure and Function of Biomolecules
Experiments on denaturation and renaturation after the reduction and reoxidation of the —S—S— bonds in the enzyme ribonuclease (RNase) have shown that:
#Question id: 911
#Unit 1. Structure and Function of Biomolecules
The correct order for molecular chaperone–mediated protein folding is:
I – exchange of ATP for ADP on chaperone
II – chaperone undergoes conformational change, which affects protein folding
III – chaperone binds to exposed hydrophobic residues on unfolded protein
IV – folded protein is released
#Question id: 912
#Unit 1. Structure and Function of Biomolecules
Which of the following is correct about the native state of a protein
a. is unaffected by changes in temperature and pH.
b. corresponds to the highest Gibbs free energy state.
c. is determined by its primary amino acid sequence.
d. corresponds to the lowest entropic state.
#Question id: 913
#Unit 1. Structure and Function of Biomolecules
The appropriate folding of a newly translated product is essential, and continual misfolding often leads to disease, especially in vertebrates. This misfolding, particularly in the situation of prion diseases, may be due to
#Question id: 914
#Unit 1. Structure and Function of Biomolecules
Lipoprotein lipase acts in:
#Question id: 915
#Unit 1. Structure and Function of Biomolecules
Free fatty acids in the bloodstream are: