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 Heart2h 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

Previous problemNext problem

Struggling with Anatomy & Physiology?

Join thousands of students who trust us to help them ace their exams!Watch the first video

Multiple Choice

Enzyme molecules require a specific shape to perform their catalytic function. Which of the following might alter the shape of an enzymatic protein?

Denaturing the protein

A change in salt concentrations or pH

Heating the protein

Treating the protein with a chemical that breaks hydrogen bonds

All of the listed responses are correct.

Previous problemNext problem

Verified step by step guidance

Understand that enzymes are proteins that have a specific three-dimensional shape crucial for their function. This shape is determined by the sequence of amino acids and the interactions between them, including hydrogen bonds, ionic bonds, and hydrophobic interactions.

Recognize that denaturing a protein involves disrupting its structure without breaking its peptide bonds. This can be caused by various factors, including changes in temperature, pH, or chemical exposure, leading to a loss of function.

Consider how changes in salt concentrations or pH can affect the ionic bonds and hydrogen bonds within the protein structure. These changes can lead to alterations in the protein's shape, affecting its ability to bind substrates and perform its catalytic function.

Heating a protein can increase the kinetic energy of its molecules, potentially disrupting the weak interactions that maintain its structure, such as hydrogen bonds and van der Waals forces, leading to denaturation.

Treating a protein with chemicals that break hydrogen bonds directly affects the secondary and tertiary structures of the protein, altering its shape and potentially its function. All these factors can lead to changes in the enzyme's shape, impacting its catalytic activity.