Table of contents

1. Matter and Measurements4h 31m
2. Atoms and the Periodic Table5h 23m
3. Ionic Compounds2h 18m
4. Molecular Compounds2h 18m
5. Classification & Balancing of Chemical Reactions3h 17m
6. Chemical Reactions & Quantities2h 27m
7. Energy, Rate and Equilibrium3h 46m
8. Gases, Liquids and Solids3h 25m
9. Solutions4h 10m
10. Acids and Bases3h 29m
11. Nuclear Chemistry56m
BONUS: Lab Techniques and Procedures1h 38m
BONUS: Mathematical Operations and Functions47m
12. Introduction to Organic Chemistry1h 34m
13. Alkenes, Alkynes, and Aromatic Compounds2h 12m
14. Compounds with Oxygen or Sulfur1h 6m
15. Aldehydes and Ketones1h 1m
16. Carboxylic Acids and Their Derivatives1h 11m
17. Amines39m
18. Amino Acids and Proteins1h 51m
19. Enzymes1h 37m
20. Carbohydrates1h 41m
21. The Generation of Biochemical Energy2h 8m
22. Carbohydrate Metabolism2h 22m
23. Lipids2h 26m
24. Lipid Metabolism1h 45m
25. Protein and Amino Acid Metabolism1h 37m
26. Nucleic Acids and Protein Synthesis2h 54m

18. Amino Acids and Proteins

Tertiary Protein Structure

GOB Chemistry

18. Amino Acids and Proteins

Tertiary Protein Structure

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2:35 minutes

Problem 82d

Textbook Question

Consider the amino acids histidine, phenylalanine, and serine in an enzyme. State which of these amino acids have R groups that would:
d. form salt bridges

Verified step by step guidance

Understand the concept of salt bridges: Salt bridges are ionic interactions that occur between oppositely charged groups in molecules, such as the side chains (R groups) of amino acids. These interactions typically involve a positively charged group (e.g., an amino group) and a negatively charged group (e.g., a carboxylate group).

Examine the R group of histidine: Histidine has an imidazole group in its side chain, which can gain a proton under physiological pH, making it positively charged. This allows histidine to participate in salt bridge formation with negatively charged groups.

Examine the R group of phenylalanine: Phenylalanine has a nonpolar benzyl group in its side chain. Since it is nonpolar and lacks a charge, it cannot form salt bridges.

Examine the R group of serine: Serine has a hydroxymethyl group (-CH2OH) in its side chain. This group is polar but uncharged, so serine cannot form salt bridges.

Conclude which amino acids can form salt bridges: Based on the analysis, histidine is the only amino acid among the three that has an R group capable of forming salt bridges due to its ability to carry a positive charge under physiological conditions.

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Key Concepts

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

Amino Acid R Groups

Amino acids have unique side chains, known as R groups, that determine their properties and interactions. These R groups can be polar, nonpolar, acidic, or basic, influencing how amino acids behave in proteins. Understanding the nature of these R groups is essential for predicting how they will interact with each other and with the environment.

Salt Bridges

Salt bridges are non-covalent interactions that occur between positively and negatively charged R groups of amino acids. They play a crucial role in stabilizing protein structures and are particularly important in enzyme function. Identifying which amino acids can form salt bridges helps in understanding the overall stability and activity of the enzyme.

Enzyme Structure and Function

The structure of an enzyme is intricately linked to its function, with specific amino acids contributing to the active site and overall stability. The arrangement of R groups affects how substrates bind and how the enzyme catalyzes reactions. Recognizing the role of specific amino acids in enzyme activity is vital for comprehending biochemical processes.

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Identify the amino acids and type of interaction that occurs between the following R groups in tertiary protein structures:

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Identify the amino acids and type of interaction that occurs between the following R groups in tertiary protein structures:

c. —CH₂—SH and HS—CH₂—

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Textbook Question

What type of interaction would you expect between the following in a tertiary structure?

a. threonine and glutamine

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If glutamate were replaced by proline in a protein, how might the tertiary structure be affected?

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Textbook Question

What type of interaction would you expect between the R groups of the following amino acids in a tertiary structure?

c. serine and aspartate

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Textbook Question

In myoglobin, about one-half of the 153 amino acids have nonpolar R groups.

a. Where would you expect those amino acids to be located in the tertiary structure?

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Textbook Question

In myoglobin, about one-half of the 153 amino acids have nonpolar R groups.

b. Where would you expect the polar R groups to be in the tertiary structure?

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Textbook Question

When a protein folds into its tertiary structure, does the primary structure change? Explain.

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Consider the amino acids histidine, phenylalanine, and serine in an enzyme. State which of these amino acids have R groups that would:d. form salt bridges

Key Concepts

Amino Acid R Groups

Salt Bridges

Enzyme Structure and Function

Watch next

Consider the amino acids histidine, phenylalanine, and serine in an enzyme. State which of these amino acids have R groups that would:
d. form salt bridges