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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1:45 minutes

Problem 2

Textbook Question

What type of bond is directly involved in the formation of an α-helix?a. peptide bonds between amino acid residuesb. hydrogen bonds between amino acid residuesc. van der Waals interactions between nonpolar residuesd. disulfide bonds between cysteine residues

Verified step by step guidance

Identify the structure in question: the α-helix is a common secondary structure in proteins.

Understand that secondary structures are stabilized by interactions between the backbone atoms of the polypeptide chain.

Recall that peptide bonds are covalent bonds that link amino acids together in a chain, forming the primary structure, not the secondary structure.

Consider the role of hydrogen bonds, which often stabilize secondary structures like α-helices by forming between the carbonyl oxygen of one amino acid and the amide hydrogen of another.

Recognize that van der Waals interactions and disulfide bonds are not typically involved in the formation of α-helices; van der Waals interactions are weak and non-specific, while disulfide bonds are covalent and stabilize tertiary structures.

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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 during a dehydration synthesis reaction, where the carboxyl group of one amino acid reacts with the amino group of another, releasing a molecule of water. While peptide bonds are crucial for the primary structure of proteins, they do not directly stabilize secondary structures like the α-helix.

Hydrogen Bonds

Hydrogen bonds are weak attractions that occur between a hydrogen atom covalently bonded to an electronegative atom and another electronegative atom. In the context of an α-helix, hydrogen bonds form between the carbonyl oxygen of one amino acid and the amide hydrogen of another, stabilizing the helical structure. This interaction is essential for maintaining the secondary structure of proteins.

Secondary Structure

Secondary structure refers to the local folded structures that form within a protein due to interactions between the backbone atoms. Common types include α-helices and β-sheets, which are stabilized by hydrogen bonds. Understanding secondary structure is vital for grasping how proteins achieve their functional shapes and how these shapes relate to their biological roles.