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

Chaperone Proteins

Biochemistry

4. Protein Structure

Chaperone Proteins

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Multiple Choice

Which statement most accurately characterizes the effect of high temperatures (>50˚C) on protein folding?

High temperatures increase the rate of protein folding so proteins adopt their native fold faster.

There is little to no effect of high temperature on protein folding.

At high temperatures, proteins are denatured but will re-fold into their native state upon cooling.

At high temperatures, proteins are denatured and at risk of forming intermolecular aggregates.

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Verified step by step guidance

Understand the concept of protein folding: Proteins fold into specific three-dimensional structures that are crucial for their function. This folding is driven by interactions such as hydrogen bonds, hydrophobic interactions, and van der Waals forces.

Recognize the impact of temperature on protein structure: High temperatures can disrupt the non-covalent interactions that stabilize the protein's native structure, leading to denaturation.

Define denaturation: Denaturation refers to the loss of the native structure of a protein, which often results in loss of function. This process is typically irreversible at high temperatures.

Consider the risk of aggregation: When proteins are denatured, they may expose hydrophobic regions that can lead to intermolecular interactions, causing aggregation. Aggregates are often non-functional and can be detrimental to cellular processes.

Conclude the effect of high temperatures: High temperatures (>50˚C) generally lead to protein denaturation and increase the risk of forming intermolecular aggregates, rather than promoting faster folding or having little effect.