What is the primary function of ubiquitination in cells?
Ubiquitination of Damaged Proteins

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1.
MULTIPLE CHOICE QUESTION
30 sec • 1 pt
To increase protein stability
To enhance protein synthesis
To signal the degradation of damaged proteins
To facilitate protein folding
2.
MULTIPLE CHOICE QUESTION
30 sec • 1 pt
Which enzyme is responsible for attaching ubiquitin to the damaged protein?
Proteasome
E3
E2
E1
3.
MULTIPLE CHOICE QUESTION
30 sec • 1 pt
What is the role of E1 in the ubiquitination process?
It activates ubiquitin by attaching an adenosine monophosphate
It degrades the ubiquitinated protein
It transports ubiquitin to the proteasome
It directly attaches ubiquitin to the damaged protein
4.
MULTIPLE CHOICE QUESTION
30 sec • 1 pt
Why is ATP necessary in the ubiquitination process?
To degrade the ubiquitinated protein
To provide energy for the formation of a thioester bond
To stabilize the ubiquitin molecule
To directly attach ubiquitin to lysine residues
5.
MULTIPLE CHOICE QUESTION
30 sec • 1 pt
What is polyubiquitination?
The attachment of multiple ubiquitin molecules to a protein
The degradation of ubiquitin molecules
The attachment of a single ubiquitin molecule to a protein
The removal of ubiquitin from a protein
6.
MULTIPLE CHOICE QUESTION
30 sec • 1 pt
What is the role of the proteasome in the cell?
To synthesize new proteins
To transport proteins across the cell membrane
To attach ubiquitin to proteins
To degrade polyubiquitinated proteins
7.
MULTIPLE CHOICE QUESTION
30 sec • 1 pt
What happens to the amino acids after a protein is degraded by the proteasome?
They are used to produce energy
They are stored in the cell
They are excreted from the cell
They are recycled to build new proteins
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