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

1. Introduction to Biochemistry

Proteins

Biochemistry

1. Introduction to Biochemistry

Proteins

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Multiple Choice

Which of the following actions or activities will NOT cause a protein’s structure to break down (denature)?

Heating the protein to 95°C

Adding a strong acid such as HCl

Storing the protein at 4°C (refrigeration)

Exposing the protein to high concentrations of urea

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Verified step by step guidance

Step 1: Understand the concept of protein denaturation. Protein denaturation refers to the process where a protein loses its native structure due to the disruption of non-covalent interactions such as hydrogen bonds, ionic bonds, and hydrophobic interactions. This process often leads to the loss of biological function.

Step 2: Analyze the effects of heating. Heating a protein to 95°C provides enough thermal energy to disrupt hydrogen bonds and other weak interactions, leading to denaturation.

Step 3: Examine the impact of adding a strong acid like HCl. Strong acids can alter the pH of the environment, disrupting ionic bonds and hydrogen bonds within the protein, which can lead to denaturation.

Step 4: Consider the effect of exposing the protein to high concentrations of urea. Urea is a chaotropic agent that disrupts hydrogen bonds and hydrophobic interactions, causing the protein to unfold and denature.

Step 5: Evaluate the effect of storing the protein at 4°C. Refrigeration at 4°C is a mild condition that does not disrupt the non-covalent interactions within the protein. Therefore, this action does NOT cause denaturation and helps preserve the protein's structure.