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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Problem 4

Textbook Question

The structural level of a protein least affected by a disruption in hydrogen bonding is thea. primary level.b. secondary level.c. tertiary level.d. quaternary level.

Verified step by step guidance

Understand the structure of proteins, which are made up of amino acids linked by peptide bonds forming a polypeptide chain.

Recognize that the primary structure of a protein is its unique sequence of amino acids in the polypeptide chain, which is held together by peptide bonds.

Identify that the secondary structure includes alpha helices and beta sheets, which are stabilized by hydrogen bonds between the backbone atoms in the polypeptide chain.

Note that the tertiary structure is the overall three-dimensional shape of a single polypeptide chain, stabilized by various interactions including hydrogen bonds, ionic bonds, hydrophobic interactions, and disulfide bridges.

Acknowledge that the quaternary structure involves the arrangement of multiple polypeptide subunits, which are also stabilized by interactions similar to those in 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. The primary structure is the sequence of amino acids, while the secondary structure refers to local folding patterns like alpha helices and beta sheets. Tertiary structure is the overall 3D shape of a single polypeptide chain, and quaternary structure involves the assembly of multiple polypeptide chains into a functional protein.

Hydrogen Bonding in Proteins

Hydrogen bonds are weak interactions that play a crucial role in stabilizing the secondary and tertiary structures of proteins. They form between polar side chains and contribute to the folding and stability of the protein. Disruption of hydrogen bonds can lead to denaturation, affecting the protein's shape and function, particularly at the secondary and tertiary levels.

Stability of Primary Structure

The primary structure of a protein, which is the linear sequence of amino acids, is held together by covalent peptide bonds. This structure is the least affected by disruptions in hydrogen bonding, as it does not rely on these interactions for its integrity. Therefore, changes in hydrogen bonding primarily impact higher levels of protein structure, such as secondary and tertiary.