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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3:47 minutes

Problem 71d

Textbook Question

Identify the level of protein structure associated with each of the following:
d. intermolecular forces between R groups

Verified step by step guidance

Understand that proteins have four levels of structure: primary, secondary, tertiary, and quaternary. Each level describes a different aspect of the protein's organization.

Recall that the tertiary structure of a protein refers to the three-dimensional folding of the polypeptide chain, which is stabilized by interactions between the R groups (side chains) of amino acids.

Recognize that intermolecular forces between R groups include hydrogen bonding, ionic interactions, hydrophobic interactions, and disulfide bonds. These forces contribute to the overall shape and stability of the protein's tertiary structure.

Differentiate this from the quaternary structure, which involves interactions between multiple polypeptide chains, and the secondary structure, which involves local folding patterns like alpha-helices and beta-sheets stabilized by hydrogen bonds in the backbone.

Conclude that the level of protein structure associated with intermolecular forces between R groups is the tertiary structure.

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Key Concepts

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

Protein Structure Levels

Proteins have four levels of structure: primary, secondary, tertiary, and quaternary. Each level represents a different aspect of protein organization, from the sequence of amino acids to the overall three-dimensional shape formed by interactions between multiple polypeptide chains.

Tertiary Structure

The tertiary structure of a protein refers to its overall three-dimensional shape, which is formed by the folding of the polypeptide chain. This folding is driven by interactions among the R groups (side chains) of the amino acids, including hydrogen bonds, ionic bonds, hydrophobic interactions, and disulfide bridges.

Intermolecular Forces

Intermolecular forces are the attractive forces between molecules or different parts of a molecule. In the context of proteins, these forces, such as hydrogen bonds and van der Waals forces, play a crucial role in stabilizing the tertiary structure by influencing how R groups interact with each other and with the surrounding environment.

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Identify the level of protein structure associated with each of the following:d. intermolecular forces between R groups

Key Concepts

Protein Structure Levels

Tertiary Structure

Intermolecular Forces

Watch next

Identify the level of protein structure associated with each of the following:
d. intermolecular forces between R groups