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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Multiple Choice

Which of the following statements concerning protein structure is incorrect?

Primary structure refers to the sequence of amino acids in a protein.

Secondary structure is stabilized by hydrogen bonds between the backbone atoms.

Tertiary structure is determined by interactions between R groups of amino acids.

Quaternary structure is the linear sequence of amino acids in a polypeptide chain.

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Verified step by step guidance

Understand the four levels of protein structure: primary, secondary, tertiary, and quaternary.

Primary structure is the linear sequence of amino acids in a protein, held together by peptide bonds.

Secondary structure refers to local folded structures that form within a polypeptide due to interactions between atoms of the backbone. The most common types are alpha helices and beta sheets, stabilized by hydrogen bonds.

Tertiary structure is the overall three-dimensional shape of a single protein molecule, formed by interactions between the R groups (side chains) of the amino acids, including hydrogen bonds, ionic bonds, disulfide bridges, and hydrophobic interactions.

Quaternary structure involves the assembly of multiple polypeptide chains into a functional protein complex. It is not about the linear sequence of amino acids, but rather the arrangement and interaction of multiple subunits.