Table of contents

1. Introduction to Anatomy & Physiology5h 43m
2. Cell Chemistry & Cell Components12h 36m
3. Energy & Cell Processes10h 6m
4. Tissues & Histology10h 3m
5. Integumentary System2h 20m
6. Bones & Skeletal Tissue2h 16m
7. The Skeletal System2h 35m
8. Joints2h 17m
9. Muscle Tissue2h 33m
10. Muscles1h 11m
11. Nervous Tissue and Nervous System1h 35m
12. The Central Nervous System1h 6m
- Introduction to the Central Nervous System
  18m
- The Cerebrum
  48m
13. The Peripheral Nervous System1h 26m
14. The Autonomic Nervous System1h 38m
15. The Special Senses2h 41m
16. The Endocrine System2h 48m
17. The Blood3h 22m
18. The Heart3h 42m
19. The Blood Vessels3h 35m
20. The Lymphatic System3h 16m
21. The Immune System14h 37m
22. The Respiratory System3h 20m
23. The Digestive System2h 5m
24. Metabolism and Nutrition4h 0m
25. The Urinary System2h 39m
26. Fluid and Electrolyte Balance, Acid Base Balance37m
27. The Reproductive System2h 5m
28. Human Development1h 21m
29. Heredity3h 32m

2. Cell Chemistry & Cell Components

Introduction to Biomolecules

Anatomy & Physiology

2. Cell Chemistry & Cell Components

Introduction to Biomolecules

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Multiple Choice

Where would a hydrophobic amino acid R group (side group) most likely be found in a properly folded protein?

On the exterior surface of the protein, interacting with water

In the interior of the protein, away from water

In the active site of the protein, interacting with substrates

On the surface of the protein, interacting with polar molecules

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Verified step by step guidance

Understand the nature of hydrophobic amino acids: Hydrophobic amino acids have side chains that do not interact favorably with water. They tend to avoid aqueous environments.

Consider the structure of a protein: Proteins are composed of amino acids that fold into specific three-dimensional shapes. This folding is influenced by the properties of the amino acids, including their hydrophobic or hydrophilic nature.

Analyze the environment within a folded protein: In a properly folded protein, hydrophobic amino acids are typically found in the interior of the protein structure. This positioning minimizes their exposure to water, which is energetically favorable.

Evaluate the options given: The exterior surface of a protein is usually in contact with water, making it an unfavorable location for hydrophobic amino acids. The active site may interact with substrates, but it is not necessarily hydrophobic. The surface interacting with polar molecules is also not ideal for hydrophobic residues.

Conclude the most likely location: Based on the properties of hydrophobic amino acids and protein folding, the interior of the protein, away from water, is the most likely location for hydrophobic amino acid side groups.