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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3:37 minutes

Problem 24a

Textbook Question

In myoglobin, about one-half of the 153 amino acids have nonpolar R groups.
a. Where would you expect those amino acids to be located in the tertiary structure?

Verified step by step guidance

Understand the nature of nonpolar R groups: Nonpolar R groups are hydrophobic, meaning they tend to avoid water and prefer to interact with other nonpolar molecules or regions.

Recall the structure of myoglobin: Myoglobin is a globular protein with a tertiary structure, meaning it folds into a compact, three-dimensional shape. This folding is influenced by the interactions of amino acid side chains with their environment.

Consider the environment of the protein: In an aqueous (water-based) environment, hydrophobic (nonpolar) amino acids tend to cluster together in the interior of the protein to avoid contact with water. This is known as the hydrophobic effect.

Predict the location of nonpolar amino acids: Based on the hydrophobic effect, the nonpolar amino acids in myoglobin are most likely located in the interior of the protein, where they are shielded from the surrounding water.

Relate this to protein stability: The clustering of nonpolar amino acids in the interior contributes to the stability of the protein's tertiary structure by minimizing unfavorable interactions with water and maximizing favorable interactions among nonpolar groups.

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Key Concepts

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

Tertiary Structure of Proteins

The tertiary structure of a protein refers to its three-dimensional shape formed by the folding and interactions of its amino acid chains. This structure is stabilized by various interactions, including hydrogen bonds, ionic bonds, and hydrophobic interactions. Understanding the tertiary structure is crucial for predicting how proteins function and interact with other molecules.

Hydrophobic and Hydrophilic Interactions

Hydrophobic interactions occur when nonpolar R groups of amino acids cluster together to avoid contact with water, while hydrophilic interactions involve polar R groups that are attracted to water. In the context of protein structure, nonpolar amino acids are typically found in the interior of the protein, away from the aqueous environment, which helps maintain the protein's stability and functionality.

Amino Acid Properties

Amino acids are the building blocks of proteins, and their properties are determined by their R groups (side chains). Nonpolar R groups are hydrophobic and tend to be located in the interior of proteins, while polar or charged R groups are hydrophilic and often found on the surface. Recognizing these properties is essential for understanding how amino acids contribute to the overall structure and behavior of proteins.

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