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

Tertiary Protein Structure

GOB Chemistry

18. Amino Acids and Proteins

Tertiary Protein Structure

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3:13 minutes

Problem 27b

Textbook Question

What type of interaction would you expect between the side chains of each of the following pairs of amino acids in the tertiary structure of a protein?
b. leucine and isoleucine

Verified step by step guidance

Identify the side chains of leucine and isoleucine. Both are nonpolar and hydrophobic.

Understand that nonpolar side chains tend to interact through hydrophobic interactions.

In the tertiary structure of a protein, hydrophobic side chains like those of leucine and isoleucine will likely cluster together to avoid water.

These interactions help stabilize the protein's structure by minimizing the exposure of hydrophobic side chains to the aqueous environment.

Conclude that the interaction between leucine and isoleucine side chains is primarily hydrophobic in nature.

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Key Concepts

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

Amino Acid Side Chains

Amino acids have unique side chains (R groups) that determine their chemical properties and interactions. These side chains can be polar, nonpolar, acidic, or basic, influencing how amino acids interact with each other in a protein's tertiary structure. Understanding the nature of these side chains is crucial for predicting interactions between specific amino acids.

Hydrophobic Interactions

Hydrophobic interactions occur when nonpolar side chains, such as those of leucine and isoleucine, cluster together to avoid contact with water. This phenomenon is a key driving force in the folding of proteins, as it helps stabilize the tertiary structure by minimizing the exposure of hydrophobic regions to the aqueous environment.

Protein Tertiary Structure

The tertiary structure of a protein refers to its three-dimensional shape formed by the folding of its polypeptide chain. This structure is stabilized by various interactions, including hydrophobic interactions, hydrogen bonds, ionic bonds, and disulfide bridges. The specific arrangement of amino acids, including leucine and isoleucine, plays a significant role in determining the overall stability and functionality of the protein.

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Textbook Question

In myoglobin, about one-half of the 153 amino acids have nonpolar R groups.

b. Where would you expect the polar R groups to be in the tertiary structure?

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Textbook Question

When a protein folds into its tertiary structure, does the primary structure change? Explain.

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Textbook Question

What type of interaction would you expect between the side chains of each of the following pairs of amino acids in the tertiary structure of a protein?

b. alanine and valine

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Textbook Question

What type of interaction would you expect between the side chains of each of the following pairs of amino acids in the tertiary structure of a protein?

a. lysine and glutamate

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Textbook Question

What type of interaction would you expect between the side chains of each of the following pairs of amino acids in the tertiary structure of a protein?

d. glutamine and arginine

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Textbook Question

Myoglobin is a protein containing 153 amino acids. Approximately half of the amino acids in myoglobin have polar side chains.

a. Where would you expect these amino acid side chains to be located in the tertiary structure of the protein?

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Textbook Question

Myoglobin is a protein containing 153 amino acids. Approximately half of the amino acids in myoglobin have polar side chains.

b. Where would you expect the nonpolar side chains to be?

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Textbook Question

Would you expect to find this segment at the center or on the surface of a globular protein? Why?

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What type of interaction would you expect between the side chains of each of the following pairs of amino acids in the tertiary structure of a protein?b. leucine and isoleucine

Key Concepts

Amino Acid Side Chains

Hydrophobic Interactions

Protein Tertiary Structure

Watch next

What type of interaction would you expect between the side chains of each of the following pairs of amino acids in the tertiary structure of a protein?
b. leucine and isoleucine