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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2:42 minutes

Problem 68

Textbook Question

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

Verified step by step guidance

Understand that the tertiary structure of a protein refers to the three-dimensional folding of the protein chain, which is stabilized by various interactions and bonds.

Recall that covalent bonds are strong chemical bonds formed by the sharing of electron pairs between atoms.

Identify the specific covalent bond that stabilizes the tertiary structure of proteins: the disulfide bond (also called a disulfide bridge).

Explain that disulfide bonds form between the sulfur atoms of two cysteine amino acid residues in the protein, creating a covalent linkage (S-S bond).

Conclude that disulfide bonds are crucial for maintaining the stability and proper folding of the protein's tertiary structure, especially in extracellular proteins.

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Key Concepts

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

Covalent Bonds

Covalent bonds are strong chemical bonds formed when two atoms share electrons. In proteins, these bonds are crucial for maintaining structural integrity. The most relevant covalent bond in the context of protein structure is the disulfide bond, which forms between the sulfur atoms of cysteine residues, providing stability to the protein's tertiary structure.

Tertiary Structure of Proteins

The tertiary structure of a protein refers to its three-dimensional shape, which is essential for its function. This structure is formed by the folding and interactions of the protein's secondary structures (like alpha helices and beta sheets) and is stabilized by various interactions, including hydrogen bonds, ionic bonds, and covalent bonds such as disulfide bridges.

Disulfide Bonds

Disulfide bonds are a specific type of covalent bond that occurs between the thiol groups of cysteine residues in proteins. These bonds play a critical role in stabilizing the tertiary structure by linking different parts of the protein chain, thus helping to maintain its functional conformation under varying environmental conditions.

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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

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

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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Textbook Question

Interactions of amino acids on the interior of proteins are key to the shapes of proteins. In group (a), which pairs of amino acids form hydrophobic interactions? In group (b), which pairs form ionic interactions? Which pairs in group (c) form hydrogen bonds?

a. 1 Pro . . . Phe

2 Lys . . . Ser

3 Thr . . . Leu

4 Ala . . . Gly

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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?