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1. Introduction to Biochemistry4h 34m
2. Water3h 23m
3. Amino Acids8h 10m
4. Protein Structure10h 4m
5. Protein Techniques14h 5m
6. Enzymes and Enzyme Kinetics13h 38m
7. Enzyme Inhibition and Regulation 8h 42m
8. Protein Function 9h 41m
9. Carbohydrates7h 49m
10. Lipids5h 49m
11. Biological Membranes and Transport 6h 37m
12. Biosignaling9h 45m
Review 1: Nucleic Acids, Lipids, & Membranes2h 47m
Review 2: Biosignaling, Glycolysis, Gluconeogenesis, & PP-Pathway3h 12m
Review 3: Pyruvate & Fatty Acid Oxidation, Citric Acid Cycle, & Glycogen Metabolism2h 26m
Review 4: Amino Acid Oxidation, Oxidative Phosphorylation, & Photophosphorylation1h 48m

7. Enzyme Inhibition and Regulation

Ubiquitination

Biochemistry

7. Enzyme Inhibition and Regulation

Ubiquitination

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Multiple Choice

_____ involves covalent attachment of peptides leading to _ of the target protein by ____.

Ubiquitination ; Activation ; Proteasome.

Glycosylation ; Degradation ; Ribosome.

Ubiquitination ; Degradation ; Proteome.

Ubiquitination ; Degradation ; Proteasome.

Acetylation ; Activation ; Proteasome.

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Verified step by step guidance

Identify the process described: The problem involves the covalent attachment of peptides to a target protein, which is a key feature of ubiquitination.

Understand the outcome of the process: Ubiquitination typically leads to the degradation of the target protein.

Determine the cellular machinery involved: The degradation of ubiquitinated proteins is carried out by the proteasome.

Match the descriptions to the options provided: The correct sequence is 'Ubiquitination ; Degradation ; Proteasome'.

Review the incorrect options: Glycosylation involves sugar attachment, not peptides. Acetylation involves acetyl groups, not leading to degradation by the proteasome.