Table of contents

1. Matter and Measurements4h 31m
2. Atoms and the Periodic Table5h 23m
3. Ionic Compounds2h 18m
4. Molecular Compounds2h 18m
5. Classification & Balancing of Chemical Reactions3h 17m
6. Chemical Reactions & Quantities2h 27m
7. Energy, Rate and Equilibrium3h 46m
8. Gases, Liquids and Solids3h 25m
9. Solutions4h 10m
10. Acids and Bases3h 29m
11. Nuclear Chemistry56m
BONUS: Lab Techniques and Procedures1h 38m
BONUS: Mathematical Operations and Functions47m
12. Introduction to Organic Chemistry1h 34m
13. Alkenes, Alkynes, and Aromatic Compounds2h 12m
14. Compounds with Oxygen or Sulfur1h 6m
15. Aldehydes and Ketones1h 1m
16. Carboxylic Acids and Their Derivatives1h 11m
17. Amines39m
18. Amino Acids and Proteins1h 51m
19. Enzymes1h 37m
20. Carbohydrates1h 41m
21. The Generation of Biochemical Energy2h 8m
22. Carbohydrate Metabolism2h 22m
23. Lipids2h 26m
24. Lipid Metabolism1h 45m
25. Protein and Amino Acid Metabolism1h 37m
26. Nucleic Acids and Protein Synthesis2h 54m

18. Amino Acids and Proteins

Summary of Protein Structure

GOB Chemistry

18. Amino Acids and Proteins

Summary of Protein Structure

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Problem 93c

Textbook Question

Explain how a protein is denatured by the following:
c. Organic solvents

Verified step by step guidance

Understand the concept of protein denaturation: Denaturation is the process in which a protein loses its native three-dimensional structure due to the disruption of non-covalent interactions, such as hydrogen bonds, ionic bonds, and hydrophobic interactions. This process does not break peptide bonds but alters the protein's functional shape.

Recognize the role of organic solvents: Organic solvents, such as ethanol or acetone, are capable of disrupting the hydrophobic interactions within a protein. These interactions are critical for maintaining the protein's tertiary structure, as hydrophobic side chains are typically buried in the interior of the protein to avoid contact with water.

Explain the mechanism of disruption: Organic solvents reduce the polarity of the surrounding environment, making it less favorable for hydrophobic side chains to remain buried. This causes the hydrophobic regions of the protein to unfold and become exposed to the solvent, leading to a loss of the protein's native structure.

Consider the impact on hydrogen bonding: Organic solvents can also interfere with hydrogen bonding by competing with water molecules or directly interacting with polar groups in the protein. This further destabilizes the protein's secondary and tertiary structures.

Summarize the result: The combined effects of disrupted hydrophobic interactions and hydrogen bonding lead to the unfolding of the protein, rendering it non-functional. This process is reversible or irreversible depending on the specific protein and conditions.

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Key Concepts

Here are the essential concepts you must grasp in order to answer the question correctly.

Protein Structure

Proteins are composed of long chains of amino acids that fold into specific three-dimensional structures. These structures are crucial for their function and are categorized into four levels: primary, secondary, tertiary, and quaternary. The stability of these structures is maintained by various interactions, including hydrogen bonds, ionic bonds, and hydrophobic interactions.

Denaturation

Denaturation refers to the process where a protein loses its native structure due to external stressors, such as heat, pH changes, or chemical agents. This alteration disrupts the interactions that maintain the protein's shape, leading to a loss of function. Denatured proteins may aggregate or precipitate, rendering them biologically inactive.

Organic Solvents

Organic solvents, such as ethanol or acetone, can disrupt the hydrophobic interactions within proteins. These solvents can solvate nonpolar amino acid side chains, leading to the unfolding of the protein structure. The presence of organic solvents can also alter the protein's environment, further promoting denaturation and affecting its solubility and functionality.

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Determine whether each of the following statements describes the primary, secondary, tertiary, or quaternary structure of a protein.

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Determine whether each of the following statements describes the primary, secondary, tertiary, or quaternary structure of a protein.

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Determine whether each of the following statements describes the primary, secondary, tertiary, or quaternary structure of a protein.

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Explain how a protein is denatured by the following:c. Organic solvents

Key Concepts

Protein Structure

Denaturation

Organic Solvents

Watch next

Explain how a protein is denatured by the following:
c. Organic solvents