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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2:18 minutes

Problem 79a

Textbook Question

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

Verified step by step guidance

Step 1: Understand the context of the problem. Collagen is a structural protein in the body, and it contains a modified form of a naturally occurring amino acid. The question asks us to identify the natural amino acid that is modified in collagen.

Step 2: Recall that the most common modified amino acid in collagen is hydroxyproline. Hydroxyproline is derived from the natural amino acid proline through a post-translational modification process.

Step 3: Recognize that proline is a naturally occurring amino acid with the chemical formula C₅H₉NO₂. It is unique because its side chain forms a cyclic structure, making it an imino acid.

Step 4: Understand that the modification involves the addition of a hydroxyl (-OH) group to the proline molecule, specifically at the 4th carbon of the pyrrolidine ring, resulting in hydroxyproline.

Step 5: Conclude that the natural amino acid associated with the modified form in collagen is proline.

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Key Concepts

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

Collagen Structure

Collagen is a structural protein that is a major component of connective tissues in the body. It is composed of amino acids, primarily glycine, proline, and hydroxyproline. The unique triple-helix structure of collagen provides strength and support to tissues, making it essential for skin, bones, and cartilage.

Amino Acids

Amino acids are organic compounds that serve as the building blocks of proteins. There are 20 standard amino acids, each with a specific side chain that determines its properties. Among these, glycine is the simplest and most abundant amino acid in collagen, playing a crucial role in its stability and structure.

Hydroxyproline

Hydroxyproline is a modified form of the amino acid proline, formed by the addition of a hydroxyl group. This modification is critical for collagen stability, as it allows for the formation of hydrogen bonds between collagen fibers, enhancing the structural integrity of connective tissues. Hydroxyproline is not found in significant amounts in most proteins, making it unique to collagen.

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

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