Table of contents

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

4. Protein Structure

Protein Folding

Biochemistry

4. Protein Structure

Protein Folding

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Multiple Choice

What does the three-dimensional shape of a folded polypeptide primarily determine?

The sequence of nucleotides in the gene encoding the protein

The biological function of the protein

The rate at which the protein is synthesized

The number of disulfide bonds present in the protein

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Verified step by step guidance

Understand that the three-dimensional shape of a folded polypeptide is referred to as its tertiary structure, which is crucial for its biological function.

Recall that the biological function of a protein is determined by its ability to interact with other molecules, which depends on the specific arrangement of amino acid side chains in the folded structure.

Recognize that the sequence of nucleotides in the gene encoding the protein determines the primary structure (amino acid sequence), but not directly the three-dimensional shape or biological function.

Note that the rate of protein synthesis is influenced by factors such as ribosome activity and mRNA availability, not the folded shape of the protein.

Understand that while disulfide bonds contribute to the stability of the protein's structure, the number of disulfide bonds does not solely determine the biological function of the protein.