Table of contents

1. Matter and Measurements4h 29m
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 35m
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. Amines38m
18. Amino Acids and Proteins1h 51m
19. Enzymes1h 37m
20. Carbohydrates1h 46m
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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Multiple Choice

Which of the following amino acid pairs can form a salt bridge?

Cysteine – methionine

Serine – glutamine

Valine – isoleucine

Lysine – glutamate

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Textbook Question

What kind of bond would you expect between the side chains of the following amino acids?

c. Aspartic acid and asparagine

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Textbook Question

What kind of bond would you expect between the side chains of the following amino acids?

b. Alanine and leucine

200

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Textbook Question

Is the bond formed between each pair in Problem 18.76 covalent or noncovalent?

202

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Textbook Question

For each amino acid listed, tell whether its influence on tertiary structure is largely through hydrophobic interactions, hydrogen bonding, formation of salt bridges, covalent bonding, or some combination of these effects.

a. Tyrosine

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Textbook Question

Oxytocin is a small peptide that is used to induce labor by causing contractions in uterine walls. It has the primary structure Cys-Tyr-Ile-Gln-Asn-Cys-Pro-Leu-Gln. This peptide is held in a cyclic configuration by a disulfide bridge. Draw a diagram of oxytocin, showing the disulfide bridge.

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Textbook Question

How do the following noncovalent interactions help to stabilize the tertiary and quaternary structure of a protein? Give an example of a pair of amino acids that could give rise to each interaction.

a. Hydrophobic interactions

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Textbook Question

Both α-keratin and tropocollagen have helical secondary structure. How do these molecules differ in (a) amino acid composition and (b) three-dimensional structure?

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Textbook Question

Identify the amino acids and type of interaction that occurs between the following R groups in tertiary protein structures: (16.1, 16.3)

a. <IMAGE>

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Textbook Question

Identify the amino acids and type of interaction that occurs between the following R groups in tertiary protein structures: (16.1, 16.3)

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? (16.1, 16.3)

a. threonine and glutamine

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Textbook Question

If glutamate were replaced by proline in a protein, how might the tertiary structure be affected? (16.1, 16.3)

124

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Textbook Question

Consider the amino acids histidine, phenylalanine, and serine in an enzyme. State which of these amino acids have R groups that would: (16.1, 16.3)

d. form salt bridges

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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.

112

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Textbook Question

What type of interaction would you expect between the side chains of each of the following pairs of amino acids in the tertiary structure of a protein?

b. alanine and valine

114

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Textbook Question

"What type of interaction would you expect between the side chains of each of the following pairs of amino acids in the tertiary structure of a protein?

a. lysine and glutamate"

158

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Textbook Question

What type of interaction would you expect between the side chains of each of the following pairs of amino acids in the tertiary structure of a protein?

b. leucine and isoleucine

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Textbook Question

What type of interaction would you expect between the side chains of each of the following pairs of amino acids in the tertiary structure of a protein?

d. glutamine and arginine

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Textbook Question

Myoglobin is a protein containing 153 amino acids. Approximately half of the amino acids in myoglobin have polar side chains.

a. Where would you expect these amino acid side chains to be located in the tertiary structure of the protein?

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Textbook Question

Myoglobin is a protein containing 153 amino acids. Approximately half of the amino acids in myoglobin have polar side chains.

b. Where would you expect the nonpolar side chains to be?

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Textbook Question

b. Would you expect to find this segment at the center or on the surface of a globular protein? Why?

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Textbook Question

Name the covalent bond that helps to stabilize the tertiary structure of a protein.

114

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Textbook Question

Collagen contains an amino acid that is a modified form of the naturally occurring amino acid.

a. Name the natural amino acid.

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Multiple Choice

What type of R group interaction is the most likely between the alanine and isoleucine residues?

194

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Multiple Choice

Which of the following amino acid pairs are the most likely to form hydrogen bonds?

175

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