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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0:54 minutes

Problem 14

Textbook Question

What are the two types of secondary structures found in polypeptides, and what maintains them? What stabilizes the tertiary structure of a polypeptide?

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Identify the two types of secondary structures in polypeptides: These are alpha helices and beta pleated sheets. Both structures are common forms of protein folding.

Understand what maintains these structures: The stability of alpha helices and beta pleated sheets is primarily maintained by hydrogen bonds between the carbonyl oxygen of one amino acid and the amide hydrogen of another.

Explore the tertiary structure of polypeptides: Tertiary structure refers to the overall three-dimensional shape of a polypeptide and involves more complex folding patterns of the protein chain.

Recognize what stabilizes the tertiary structure: The stability of the tertiary structure is maintained by various interactions including hydrogen bonds, ionic bonds, disulfide bridges, and hydrophobic interactions.

Consider the role of the environment: Environmental factors such as pH and temperature can affect the stability of both secondary and tertiary structures, influencing the overall conformation and function of the protein.

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Key Concepts

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

Secondary Structure of Proteins

Secondary structures in polypeptides refer to the local folded structures that form within a protein due to hydrogen bonding between the backbone atoms. The two primary types are alpha helices, which are coiled structures, and beta sheets, which are formed by parallel or antiparallel strands. These structures are crucial for the overall shape and function of proteins.

Hydrogen Bonds

Hydrogen bonds are weak interactions that occur between a hydrogen atom covalently bonded to an electronegative atom and another electronegative atom. In the context of protein secondary structures, these bonds stabilize the alpha helices and beta sheets by forming between the carbonyl oxygen of one amino acid and the amide hydrogen of another, thus maintaining the protein's shape.

Tertiary Structure of Proteins

The tertiary structure of a polypeptide refers to its overall three-dimensional shape, which is determined by the interactions among various side chains (R groups) of the amino acids. This structure is stabilized by several types of interactions, including hydrogen bonds, ionic bonds, hydrophobic interactions, and disulfide bridges, which collectively contribute to the protein's stability and functionality.