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

Proteins

Anatomy & Physiology

2. Cell Chemistry & Cell Components

Proteins

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0:45 minutes

Problem 9

Textbook Question

Based on what you know of the peptide bonds that link together amino acid residues, why would proline's side chain reduce the flexibility of the backbone?

Verified step by step guidance

Understand the structure of a peptide bond: Peptide bonds are covalent bonds that link the carboxyl group of one amino acid to the amino group of another, releasing a molecule of water. This bond forms the backbone of protein structures.

Recognize the unique structure of proline: Proline differs from other amino acids because it has a cyclic structure; its side chain is bonded to the nitrogen atom of its amino group, forming a rigid ring structure.

Consider the impact of proline's ring on the peptide bond: The ring structure of proline restricts the rotation around the N-Cα bond (the bond between the nitrogen atom and the α-carbon of the amino acid) which is normally possible in other amino acids. This restriction decreases the flexibility of the protein backbone at that point.

Compare proline with other amino acids: Most amino acids allow for free rotation around the Cα-N and Cα-C bonds due to their linear side chains, contributing to the protein's overall flexibility.

Conclude the effect of proline on protein structure: The rigidity introduced by proline's cyclic side chain limits the conformations that the protein backbone can adopt at the site of the proline residue, thus reducing the overall flexibility of the protein.

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Key Concepts

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

Peptide Bonds

Peptide bonds are covalent bonds that link amino acids together in a protein. They form between the carboxyl group of one amino acid and the amino group of another, releasing a molecule of water in a condensation reaction. This bond creates a rigid structure that contributes to the overall stability of the protein's backbone.

Amino Acid Structure

Amino acids consist of a central carbon atom bonded to an amino group, a carboxyl group, a hydrogen atom, and a variable side chain (R group). The nature of the side chain determines the properties of the amino acid, including its polarity, charge, and ability to form hydrogen bonds. Proline is unique because its side chain forms a ring structure that can influence the conformation of the protein.

Backbone Flexibility

The flexibility of a protein's backbone is crucial for its function, allowing it to adopt various conformations. Factors that affect this flexibility include the presence of certain amino acids, such as proline, which introduces a kink in the backbone due to its cyclic structure. This kink restricts rotation around the peptide bond, thereby reducing the overall flexibility of the protein.